Warianty tytułu
Języki publikacji
Abstrakty
Serine proteinases and their natural protein inhibitors belong to the most intensively studied models of protein-protein recognition. Protein inhibitors do not form a single group but can be divided into about 20 different families. Global structures of proteins representing different inhibitor families are completely different and comprise α-helical proteins, β-sheet proteins,α/β-proteins and different folds of small disulfide-rich proteins. Three different types of inhibitors can be distinguished: canonical (standard mechanism) inhibitors, non-canonical inhibitors, and serpins. The canonical inhibitor binds to the enzyme through the exposed and convex binding loop, which is complementary to the active site of the enzyme. The mechanism of inhibition in this group is consistently very similar and resembles that of an ideal substrate. Non-canonical inhibitors, originating from blood sucking organisms, specifically block enzymes of the blood clotting cascade. The interaction is mediated through inhibitor N-terminus which binds to the proteinase forming a parallel β-sheet. There are also extensive secondary interactions which provide an additional buried area and contribute significantly to the strength and specificity of recognition. Serpins are major proteinase inhibitors occurring in plasma. Similarly to canonical inhibitors, serpins interact with their target proteinases in a substrate-like manner. However, in the case of serpins, cleavage of a single peptide bond in a flexible and exposed binding loop leads to dramatic structural changes.
Wydawca
Czasopismo
Rocznik
Tom
Numer
Opis fizyczny
p.531-565,fig.
Twórcy
autor
- University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland
autor
autor
Bibliografia
- Aertgeerts, K., De Bondt, H., De Ranter, C.J. & Declerck, P.J. (1995) Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nature Struct. BioL 2, 891-897.
- Antonini, E., Ascenzi, P., Bolognesi, M., Gatti, G., Guarneri, M. & Menegatti, E. (1983) Interaction between (pro)enzyms and Kazal and Kunitz inhibitors. J. MoL BioL 165,543-558.
- Antuch, W., Berndt, K.D., Chavez, M.A., Delfin, J. & Wiithrich, K. (1993) The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus. Eur. J. Biochem. 212, 675-684.
- Antuch, W., Guntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. & Wiithrich, K. (1994) NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornthodoros moubata. FEBS Lett. 352, 251-257.
- Apostoluk, W. & Otlewski, J. (1998) Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins. Pro teins: Struct Fund. Genet. 32, 459-474.
- Ardelt, W. & Laskowski, M., Jr. (1983). Thermodynamics and kinetics of the hydrolysis and re- synthesis of the reactive site peptide bond in turkey ovomucoid third domain by asper- gillopeptidase B. Acta Biochim, Polon. 30, 115-126.
- Ardelt, W. & Laskowsk* M., Jr. (1985) Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same... Leul8 - Glul9... reactive site. Biochemistry 24, 5313-5320.
- Ardelt, W. & Laskowski, M., Jr. (1991) Effect of single amino acid replacements on the thermodynamics of the reactive site peptide bond hydrolysis in ovomucoid third domain. J. Mol Biol 220, 1041-1053.
- Ascenzi, P., Amiconi, G., Coletta, M., Lupidi, G., Menegatti, E., Onesti, S. & Bolognesi, M. (1992) Binding of hirudin to afi and y-thrombin. A comparative kinetic and thermodynamic study. J. Mol Biol 225.177-184.
- Baumann, U., Huber, R., Bode, W., Grosse, D., Lesjak, M. & Laurell, C. B. (1991a) Crystal structure of cleaved human «j-anti- chymotrypsin at 2.7 A resolution and its com parison with other serpins. J. Mol Biol 218, 595- 606.
- Baumann, U., Bode, W., Huber, R., Travis, J. & Potempa, J. (1991b) Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. J. Mol Biol 226, 1207-1218.
- Beckmann, J., Mehlich, A., Schroder, W., Wenzel, H.R. & Tschesche, H. (1988) Preparation of chemically 'mutate' aprotinin homologues by semisynthesis. P^ substitutions change inhibitory specificity. Eur. J. Biochem. 176, 675-682.
- Beeser, S.A., Goldenberg, D.P. & Oas, T.G. (1997) Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI. J. Mol Bicl 269, 154-164.
- Behnke, C.A., Yee, V.C., Trong, I.L., Pedersen, L.C., Stenkamp, R.E., Kim, S.S., Reeck, G.R. & Teller, D.C. (1998) Structural determinants of the Afunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 A resolution. Biochemistry 37, 15277-15288.
- Berndt, K.D., Guntert, P., Orbons, L.P. & Wiithrich, K. (1992) Determination of a high quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol Biol 227, 757-775.
- Betzel, C., Dauter, Z., Genov, N., Lamzin, V., Navaza, J., Schnebli, H.P., Visanji, M. & Wilson, K.P. (1993) Structure of the proteinase inhibitor eglin c with hydrolysed reactive center at 2.0 A resolution. FEBSLett. 317,185-188.
- Bjôrk, I., Ylinenjàrvi, K., Olson, S.T. & Bock, P.E. (1992) Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1-P14 region of the putative reactive bond loop of the inhibitor. J. Biol Chem. 267, 1976-1982.
- Bode, W. (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-try- psinogen J. Mol Biol 127, 357-374.
- Bode, W., Epp, O., Huber, R., Laskowski, M., Jr. & Ardelt, W. (1985) The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). Eur. J. Biochem 147, 387-395.
- Bode, W., Schwager, P. & Huber, R. (1978) The transition of bovine trypsinogen to a trypsin- like state upon ligand binding. The refined crystal structures of bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with the Ile-Val at 1.9 A resolution. J. Mol Biol 118, 99-112.
- Bode, W., Wei, A.-Z., Huber, R., Meyer, E., Travis, J. & Neuman, S. (1986a) X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of turkey ovomucoid inhibitor. EMBO J. 5, 2453-2458.
- Bode, W., Papamokos, E., Musil, D., Seemiiller, U. & Fritz, H. (1986b) Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. EMBO J. 5, 813-818.
- Bode, W., Greyling, H.J., Huber, R., Otlewski, J. & Wilusz, T. (1989) The refined 2.0 A X-ray crystal structure of the complex formed between bovine ^-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima): Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. FEBS Lett. 242, 285-292.
- Bode, W. & Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
- Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E. & Huber, R. (1982) Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. J. Mol Biol 162, 839-868.
- Bolognesi, M., Pugliese, L., Gatti, G., Frigero, F., Coda, A., Antolini, L., Schnebli, H.P., Menegatti, E., Amiconi, G. & Ascenzi, P. (1990) X-ray crystal structure of the bovine a-chymotrypsin/eglin c complex at 2.6 A resolution. J. Mol Recogn. 3, 163-168.
- Bruch, M., Weiss, V. & Engel, J. (1988) Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263, 16626-16630.
- Burgering, M.J.M., Orbons, L.P.M., van der Doelen, A., Mulders, J., Theunissen, H.J.M., Grootenhuis, P.D.J., Bode, W., Huber, R. & Stubbs, M.T. (1997) The second Kunitz domain of human tissue factor pathway inhibitor: Cloning, structure determination and interaction with factor Xa. J. Mol Biol 269, 395-407.
- Cai, M., Gong, Y., Kao, J.L.-F. & Krishnamoorthi, R. (1995a) Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 34, 5201-5211.
- Cai, M., Gong, Y., Prakash, O. & Krishnamoorthi, R. (1995b) Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: Function, thermodynamic stability, and NMR solution structure. Biochemistry 34, 12088-12094.
- Cai, M., Huang, Y., Prakaah, O., Wen, L., Dunkelbarger, S.P., Huang, J.K., Liu, J. & Krishnamoorthi, R. (1996) Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-cat&lyzed hydrolysis and NMR spectroscopy. Biochemistry 35, 4784-4794.
- Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. (1994) Biological implications of a 3 A structure of dimeric antithrombin. Structure 2, 257-270.
- Carrell, R., Lomas, D., Stein, P. & Whiststock, J. (1997) Dysfunctional variants and the structural biology of the serpins. Adv. Exp. Med. Biol 425, 207-222.
- Castro, M.J.M. & Anderson, S. (1996) Alanine pointmutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to trypsin and «-chymotrypsin. Biochemistry 35, 11435-11446.
- Chen, Z. & Bode, W. (1983) Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor: Crystallisation, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex. J. Mol Biol 164, 283-311.
- Chen, P., Rose. J., Love, R., Wei, C.H. & Wang, B.C. (1992) Reactive sites of an anticarcino- genic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors. J. Biol Chem. 267, 1990-1994.
- Chiche, L., Gaboriaud, C., Heitz, A., Mornon, J.-P., Castro, B. & Kollman, P.A. (1989) Use of restrained molecular dynamics in water to determine three dimensional protein structure: Prediction of the three dimensional structure of Ecballium elaterium trypsin inhibitor II. Proteins: Struct Fund. Genet 6, 405-417.
- Chiche, L., Heitz, A., Padilla, A., Le-Nguyen, D. & Castro, B. (1993) Solution conformation of synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: New structural alignment between the squash inhibitor and the potato carboxypepridase inhibitor. Protein Engng. 6, 675-682.
- Czapinska, H. & Otlewski, J. (1999) Structural and energetic determinants of the Sj site specificity in serine proteases. Eur. J. Biochem. 260, 571-595.
- Dattagupta, J.X., Podder, A., Chakrabarti, C., Sen, U., Mukhopadhyay, D., Dutta, S.K. & Singh, M. (1999) Refined crystal structure (2.3 A) of a double-headed winged bean al- pha-chymotrypsin inhibitor and location of its second reactive site. Proteins 35, 321-331.
- Dauter, Z., Genov, N., Pipon, N., Wilson, K.S. & Betzel, C. (1991) Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-c. Acta Cryst. B47, 707-730.
- Delarue, M., Samama, J.-P., Mourey, J.-P. & Moras, D. (1990) Crystal structure of bovine antithrombin III. Acta Crystallog. B46, 550-556.
- Dennis, M.S. & Lazarus, R.A. (1994a) Kunitz domain inhibitors of tissue factor — factor Vila: I. Potent inhibitors selected from libraries by phage display. J. Biol Chem. 269, 22129- 22136.
- Dennis, M.S. & Lazarus, R.A. (1994b) Kunitz domain inhibitors of tissue factor — factor Vila: II. Potent and specific inhibitors by competitive phage selection. J. Biol Chem. 269, 22137-22144.
- Elliott, P.R., Lomas, D.A., Carrell, R.W. & Abrahams, J.P. (1996) Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. Nature Strixt. Biol 3, 676-681.
- Engh, R., Lobermann, H., Schneider, M., Wiegand, G., Huber, R. & Laurell, C.B. (1989) The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism. Protein Engng. 2, 407-415.
- Estell, D.A., Wilson, K.A. & Laskowski, M., Jr. (1980) Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1. Biochemistry 19, 131-137.
- Finkenstadt, W.R. & Laskowski, M., Jr. (1967) Re- synthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor. J. Biol Chem. 242, 771-773.
- Finkenstadt, W.R., Hamid, M.A., Mattis, J.A., Schrode, J.A., Sealock, R.W. & Laskowski, M., Jr. (1974) Kinetics and thermodynamics of the interaction of proteinases with protein inhibitors. Bayer-Symposium V (Fritz, H., Tschesche, H., Greene, L.J. & Truscheit, E. eds.) pp. 389-411, Springer-Verlag, Berlin.
- Folkers, P.J.M., Clore, G.M., Driscoll, P.C., Dodt, J., Khler, S. & Gronenborn, A.M. (1989) Solution structure of recombinant hirudin and the Lys-47-Glu mutant: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 28, 2601-2617.
- Francart, C., Dauchez, M., Alix, A.J.P. & Lippens, G. (1997) Solution structure of R-elafin, a specific inhibitor of elastase. J. Mol Biol 268, 666-677.
- Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W.-D., Huber, R. & Bode, W. (1997) Structure of thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc. Natl Acad. ScL U.S.A. 94, 11845-11850.
- Fujinaga, M., Read, R.J., Sielecki, A., Ardelt, W., Laskowski, M., Jr. & James, M.N.G. (1982) Refined crystal structure of the molecular com plex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey. Proc. Natl Acad. SaI U.S.A. 79, 4868-4872.
- Fujinaga, M., Sielecki, A.R., Read, R.J., Ardelt, W., Laskowski, M., Jr. & James, M.N.G. (1987) Crystal and molecular structures of the complex of ff-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution. J. Mol Biol 195, 397-418.
- Gourinath, S., Srinisvasan, A. & Singh, T.P. (1999) Structure of the Afunctional inhibitor of trypsin and cr-amylase from ragi seeds at 2.9 A resolution. Acta Cryst D55, 25-30.
- Grasberger, B.L., Clore, G.M. & Gronenborn, A.M. (1994) High-resolution structure of Ascaris trypsin inhibitor in solution: Direct evidence for a pH-induced conformational transition in the reactive site. Structure 2, 669-678.
- Ureenblatt, H.M., Ryan, OA. & James, M.N.G. (1989) Structure of the complex of Strepto- myces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution. J. Mol Biol 205, 201-225.
- Gros, P., Teplyakov, A.V. & Hoi, W.G.J. (1992) Effects of eglin-c binding to thermitase: three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes. Proteins: Struct. Funct. Genet. 12, 63-70.
- Griitter, M.G., Fendrich, G., Huber, R. & Bode, W. (1988) The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine cr-chymotrypsin. EMBO J. 7, 345-351.
- Griitter, M.G., Priestle, J.P., Rahuel, J., Gross- enbacher, H., Bode, W., Hofsteenge, J. & Stone, S.R. (1990) Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition. EMBO J. 9, 2361-2365.
- Harding, L., Scott, R.H., Kellenberger, C., Hietter, H., Luu, B., Beadle, D J. & Bermudez, I. (1995) Inhibition of high voltage-activated Ca currents from cultured sensory neurones by a novel insect peptide. J. RcepL Signal Trans- duct. Res. 15, 355-364.
- Harrop, S.J., Jankova, L., Coles, M., Jardine, D., Whittaker, J.S., Gould, A.R., Meister, A., King, G.C., Mabbutt, B.C. & Curmi, P.M.G. (1999) The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: Implications for serpin function. Structure 7, 43 54.
- Heald, S.L., Tilton, R.F., Jr., Hammond, L.J., Lee, A., Bayney, R.M., Kamarck, M.E., Rama- bhadran, T.V., Dreyer, R.N., Davis, G., Unterbeck. A. & Tambutini, P.P. (1991) Sequential NMR resonance assignment and structure determination of the Kunitz-type inhibitor domain of the Alzheimer's -amyloid precursor protein. Biochemistry 30, 10467- 10478.
- Hecht, H.J., Szardenings, M., Collins. J. & Schomburg, D. (1991) Three dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). J. Mol Biol 220, 711-722.
- Hecht, H.J., Szardenings, M., Collins, J. & Schomburg, D. (1992) Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal- type). J. MoL Biol 225, 1095-1103.
- Heitz, A., Chiche, L., Le-Nguyen, D. & Castro, B. (1989) 1H 2D NMR and distance geometry study of the folding of Ecbalium elaterium trypsin inhibitor, a member of the squash inhibitor family. Biochemistry 28, 2392-2398.
- Heinz, D.W., Priestle, J.P., Rahuel, J., Wilson, K.S. & Griitter, M.G. (1991) Refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins. J. Mol Biol 217, 353-371.
- Heinz, D.W., Hyberts, S.G., Peng, J.W., Priestle, J.P., Wagner, G. & Griitter, M.G. (1992) Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: Functional and structural investigation. Biochemistry 31, 8755-8766.
- Helland, R., Leiros, I., Berglund, G.I., Willassen, N.P. & Smalas, A.O. (1998) The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur. J. Biochem. 256, 317-324.
- Helland, R., Berglund, G.I., Otlewski. J., Apostoluk, W., Andersen, O.A., Willassen, N.P. & Smalas, A.O. (1999a) High resolution crystal structures of three new trypsin-squash inhibitor complexes. Detailed comparison with other trypsins and their complexes. Acta Crysu D55, 139-148.
- Helland, R., Otlewski, J., Sundheim, O., Dadlez, M. & Smalas, A.O. (1999b) The crystal structures of the complexes between bovine /3-trypsin and ten PI variants of BPTI. J. Mol Biol 287, 923-942.
- Hipler, K., Priestle, J.P., Rahuel, J. & Grütter, M. (1992) X-ray crystal structure of the serine proteinase inhibitor eglin c at 1.95 A resolution. FEBS Lett 309, 139-145.
- Holak, T.A., Gondol, D., Otlewski, J. & Wilusz, T. (1989) Determination of the complete three- dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamic simulated annealing. J. Mol Biol 210, 635-648.
- Holak, T.A., Habazettl, J., Oschkinat, H. & Otlewski, J. (1991) Structure of proteins in solution derived from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy. High resolution structure of squash trypsin inhibitor. J. Am. Chem Soc. 113, 3196-3198.
- Hood, D.B., Huntington, J.A. & Gettins, P.G. (1994) £rrAntiproteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 33, 8538-8547.
- Huang. Q., Liu, S. & Tang, Y. (1992) Refined 1.6 A resolution crystal structure of the complex formed between porcine /J-trypsin and MCTI- A, a trypsin inhibitor of the squash family. J. Mol Biol. 229, 1022-1036.
- Huang, K., Strynadka, N.C.J., Bernard, V.D. & James, M.N.G. (1994) The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2, 669-678.
- Huang, K., Anderson, S., Laskowski, M., Jr. & James, M.N.G. (1995) Water molecules participate in proteinase-inhibitor interactions: Crystal structures of Leu 18, Ala 18 and Glyl8 variants of turkey ovomucoid inhibitor third domain coinplexed with Streptomyces griseus proteinase 3. PrvLt'ui ScL 4, 1985-1997.
- Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J. & Steigemann, W. (1974) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. J. Mol Biol 89, 73-101.
- Huber, R., Bode, W., Kukla, D., Kohl, U. & Ryan, C.A. (1975) The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Structure of the anhydro-tryp8in-inhibitor complex. Biophys. Struct Mech. 1, 189-201.
- Huber, R. & Bode, W. (1978) Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11, 114-122.
- Hurle, M.R., Marks, C.B., Kosen, P.A., Anderson, S. & Kuntz, I.D. (1990) Denaturantrdependent folding of bovine pancreatic trypsin inhibitor mutants with two-intact disulfide bonds. J. Mol Biol 29, 4410-4419.
- Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. (1992) The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comaprison with X-ray structures. Protein ScL 1, 736-751.
- Hynes, T.R., Randal, M., Kennedy, L.A., Eigenbrot, C. & Kossiakoff, A.A. (1990) X-ray crystal structure of the inhibitor domain of Alzheimer's amyloid /3-protein precursor. Biochemistry 29, 10018-10022.
- Janin, J. & Chothia, C. (1990) The structure of protein-protein recognition sites. J. Biol Chem. 265, 16027-16030.
- Jin, L., Abrahams, J.P., Skinner, R., Petitou, M., Pike, R.N. & Carrell, R.W. (1997) The anticoagulant activation of antithrombin by heparin. Proc. Natl. Acad. Sci. U.S.A. 94,14683-14688.
- Jones, S. & Thornton, J.M. (1996) Principles of protein-protein interactions. Proc. Natl. Acad Sci. U.S.A. 93, 13-20.
- Kohfeld, E., Gôhring, W., Mayer, U., Zweckstetter, M., Holak, T.A., Chu, M.-L. & Timpl, R. (1996) Conversion of the Kunitz-type module of collagen VI into a highly active trypsin inhibitor by site-directed mutagenesis. Eur. J. Biochem 238, 333-340.
- Kojima, S., Nishiyama, Y., Kumagai, I. & Miura, K. (1991) Inhibition of subtilisin BPN' by reaction site PI mutants of Streptomyces subtilisin inhibitor. J. Biochem. 109, 377-382.
- Komiyama, T., Bigler, T.L., Yoshida, N., Noda, K. & Laskowski, M., Jr. (1991) Replacement of PI Leu 18 by Glu 18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus proteinase (GluSGP). J. Biol Chem. 266, 10727-10730.
- Komiyama, T., Ray, C.A., Pickup, D.J., Howard, A.D., Thornberry, N.A., Peterson, E.P. & Salvesen, G. (1994) Inhibition of interleukin- lfi converting enzyme by the cowpox virus serpin CrmA. J. Biol Chem. 269, 19331- 19337.
- Krezel, A.M., Darba, P., Robertson, A.D., Fejzo, J., Macura, S. & Markley, J.L. (1994) Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data. J. Mol Biol 242, 203-214.
- Krokoszynska, I. & Otlewski, J. (1996) Thermodynamic stability effects of single peptide bond hydrolysis in protein inhibitors of serine proteinases. J. Mol Biol 256, 793-802.
- Krokoszynska, I., Dadlez, M. & Otlewski, J. (1998) Structure of aingle-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine /^-trypsin. J. Mol Biol 275, 503-513.
- Krowarsch, D., Dadlez, M., Buczek, O., Krokoszynska, I., Smalas, A.O. & Otlewski, J. (1999) Inter scaffolding additivity: Binding of Pj variants of bovine pancreatic trypsin inhibitor to four serine proteases. J. Mol Biol 2S9, 175-186.
- Krystek, S., Stouch, T. & Novotny, J. (1993) Affinity and specificity of serine endopeptidase- protein inhibitor interactions. J. Mol Biol 234, 661-679.
- Lapatto, R., Krengel, U., Schreuder, H.A., Arkema, A., de Boer, B., Kalk, K.H., Hoi, W.G.J., Grootenhuis, P.D.J., Mulders, J.W.M., Dijkema, R., Theunissen, H.J.M. & Dijkstra, B. W. (1997) X-ray structure of anistasin at 1.9 A resolution and its modelled complex with blood coagulation factor Xa. EMBO J. 16, 5151-5161.
- Laskowski, M., Jr. & Sealock, W.R. (1971) Protein proteinase inhibitors-molecular aspects. Enzymes 3, 376-457.
- Laskowski, M., Jr. & Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
- Laskowski, M., Jr. (1986) Protein inhibitors of serine proteinases — mechanism and classification. Adv. Exp. Med. Biol 199, 1-17.
- Laskowski, M., Jr., Kato, I., Ardelt, W., Cook, J., Denton, A., Empie, M.W., Kohr, W.J., Park, S J., Parks, K., Schatzley, B.L., Tyashiro, M., Vichot, G., Wheatley, H.E., Wieczorek, A. & Wieczorek, M. (1987) Ovomucoid third domains from 100 avian species: Isolation, sequences, and hypervariability of enzyme-inhibitor contact residues. Biochemistry 26, 202- 221.
- Lawrence, D.A. (1997) The role of reactive-center loop mobility in the serpin inhibitory mechanism. Adv. Exp. Med. Biol 425, 99-108.
- Lee, G.F., Lazarus, R.A. & Kelley, R.F. (1997) Potent Afunctional anticoagulants: Kunitz domain-tissue factor fusion proteins. Biochemistry 36, 5609-5611.
- Lee, K.N., Im, H., Kang, S.W. & Yu, M.-H. (1998) Characterization of a human a ranti trypsin variant that is as stable as ovalbumin. J. Biol Chem. 273, 2509-2516.
- Li, J., Wang, Z., Canagarajah, B., Jiang, H., Kanost, M. & Goldsmith, E.J. (1999) The structure of active serpin IK from Manduca sexta. Structure 7, 103-109.
- Li de la Sierra, 1., Quillien, L., Flecker, P., Gueguen, J. & Brunie, S. (1999) Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. J. Mol. Biol. 285, 1195-1207.
- Liepinsh, E., Berndt, K.D., Sillard, R., Mutt, V. & Otting, G. (1994) Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy. J. Mol Biol 239, 137-153.
- Lim-Wilby, M.S.L., HaUenga, K., de Maeyer, M., Lasters, I., Vlasuk, G.P. & Brunck, T.K. (1995) NMR structure determination of tick anticoagulant peptide (TAP). Protein Sci. 4,1178-1186.
- Lin, G., Bode, W., Huber, R., Chi, C. & Engh, R.A. (1993) The 0.25 nm X-ray structure of the Bowman-Birk type inhibitor from mung bean in ternary complex with porcine trypsin. Eur. J. Biochem. 212, 549-555.
- Liu, J., Praskash, O., Huang, Y., Wen, L., Wen, J.J., Huang, J.-K. & Krishnamoorthi, R. (1996a) Internal mobility of reactive-site-hy- drolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: Evidence for differential stabilization of newly formed C- and N-termini. Biochemistry 35, 12503-12510.
- Liu, J., Prakash, 0., Cai, M., Gong, Y., Huang, Y., Wen, L., Wen, J.J., Huang, J.-K. & Krishnamoorthi, R. (1996b) Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 35, 1516-1524.
- Lomas, D.A., Elliott, P.R., Chang, W.S.W., War- del1, M.R. & Carrell, R.W. (1995) Preparation and characterization of latent al-antitrypsin. J. Biol Chem. 270, 5282-5288.
- Lobermann, H., Tokuoka, R., Deisenhofer, J. & Huber, R. (1984) Human arproteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol Biol 177, 531-557.
- Lu, W., Zhang, W., Molloy, S.S., Thomas, G., Ryan, K., Chiang, Y., Anderson, S. & Laskowski, M., Jr. (1993) Arg15-Lys17-Arg18 turkey ovomucoid third domain inhibits human furin. J. Biol Chem 268,14583-14585.
- Lu, W., Qasim, M.A., Laskowski, M., Jr. & Kent, S.B.H. (1997a) Probing intermolecular main chain hydrogen bonding in serine proteinase- protein inhibitor complexes: Chemical synthesis of back-engineered turkey ovomucoid third domain. Biochemistry 36, 673-679.
- Lu, W., Apostoł, I., Qasim, M.A., Warne, N., Wynn, R., Zhang, W.L., Anderson, S., Chiang, Y.W., Ogin, E., Rothberg, I., Ryan, K. & Laskowski, M., Jr. (1997b) Binding of amino acid side chain to Si cavities of serine proteinases. J. Mcl BioL 266, 441-461.
- Ludvigsen, S., Shen, H., Kjaer, M., Madsen, J.C. & Poulsen, P.M. (1991) Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. J. Mol Biol 222, 621-635.
- Lukacs, C.M., Rubin, H. & Christianson, D.W. (1998) Engineering an anion-binding cavity in antichymotrypsin modulates the "spring- loaded" serpin-protease interaction. Biochemistry 37, 3297-3304.
- Makhatadze. G.I., Kim, K.S., Woodward, C. & Privalov, P.L. (1993) Thermodynamics of BPTI folding. Protein Sci 2, 2028-2036.
- Markland, W., Ley, A.C. & Ladner, R.C. (1996) It. erative optimization of high affinity protease inhibitors using phage display. 1. Plasmin. Biochemistry 35, 8058-8067.
- Mathialagan, N. & Hansen, T.R. (1996) Pepsin-inhibitory activity of the uterine serpins. Proc. Natl Acad. Sci U.S.A. 93,13653-13658.
- McGrath, M.E., Engel, T., Bystroff, C. & Fletterick, R.J. (1994) Macromolecular chelation as an improved mechanism: Structure of the ecotin-trypsin complex. EMBO J. 13, 1502-1507.
- McGrath, M.E., Gillmor, S.A. & Fletterick, RJ. (1995) Ecotin: Lesson on survival in a prote- ase-filled world. Protein Sci, 4, 141-148.
- McPhalen, C.A. & James, M.N.G. (1987) Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry 26, 261-269.
- McPhalen. C.A. & James, M.N.G. (1988) Structural comparison of two serine proteinase- protein inhibitor complexes: Eglin-c-subti- lisin Carlsberg and CI-2-subtilisin Novo. Biochemistry 27, 6582-6598.
- Mer, G., Kellenberger, C., Koehl, P., Stote, R., Sorokine, 0., Van Dorsselaer, A.M., Luu, B., Hietter, H. & LefvSre, J.-F. (1994) Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. Biochemistry 33, 15397-15407.
- Mer, G., Hietter, H., Kellenberger, C., Renatus, M., Luu, B. & Lefvre, J.-F. (1996) Solution structure of PMP-C: A new fold in the group of small serine proteinase inhibitors. J. Mol Biol 258, 158-171.
- Merigeau, K., Arnoux, B., Perahia, D., Norris, K. & Ducruix, A. (1998) 1.2 A of the Kunitz-type domain from the 3 chain of human type VI collagen. Acta CrysL D54, 306-312.
- Mitsui, Y., Satow, Y. & Sakamaki, T. (1977) Crystal structure of a protein protease inhibitor (Streptomyces subtilisin inhibitor) at 2.3 À resolution. J. Biochem (Tbkyo) 82, 295 298.
- Mittl, P.R.E., Di Marco, S., Fendrich, G., Pohlig, G., Heim, J., Sommerhoff, C., Fritz, H., Priestle, J.P. & Griitter, M.G. (1996) A new structural class of serine protease inhibitors revealed by the structure of the hirustasin- kallikrein complex. Structure 5, 253-264.
- Morenweiser, R., Auerswald, E.A., van de Locht, A., Fritz, H., Strzebecher, J. & Stubbs, M.T. (1997) Structure-based design of a potent chimeric thrombin inhibitor. J. Biol Chem. 272, 19938-19942.
- Moses, E. & Hinz, H.-J. (1983) Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters. J. Mol. Biol. 170, 765-776.
- Mottonen, J., Strand, A.. Symersky, J., Sweet, R.M., Danley, D.E., Geoghegan, K.F., Gerard, R.D. & Goldsmith, E.J. (1992) Structural basis of latency in plasminogen activator inhibitor-1. Nature 355, 270-273.
- Mourey, L., Samama, J.-P., Delarue, M., Petitou, M., Choay, J. & Moras, D. (1993) Crystal structure of cleaved bovine antithrombin III at 3.2 A resolution. J. Mol Biol 232, 223-241.
- Miihlhahn, P., Czisch, M., Morenweiser, R., Habermann, B., Engh, R.A., Sommerhoff, C.P., Auerswald, E.A. & Holak, T.A. (1994) Structure of leech derived tryptase inhibitor (LDTI-C) in solution. FEBS Lett. 355, 290-296.
- Musil, D., Bode, W., Huber, R., Laskowski, M., Jr., Lin, T.-Y. & Ardelt, W. (1991) Refined X-ray crystal structures of the reactive site modified ovomucoid inhibitor third domains from silver pheasant (0MSVP3*) and from Japanese quail (OMJPQ3*). J. Mol Biol 220,739-755.
- Nielsen, K.J., Alewood, D., Andrews, J., Kent, S.B.H. & Craik, D.J. (1994a) An 1H NMR determination of the three dimensional structures of mirror image forms of a Leu-5 variant of the trypsin inhibitor from Ecbalium elater- ium (EETI ID. Protein Sci. 3, 291-302.
- Nielsen, K.J., Heath, R.L., Anderson, M.A. & Craik, D.J. (1994b) The three dimensional solution structure by *H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata. J. Mol. Biol 242,231-243.
- Nielsen, K.J., Heath, R.L., Anderson, MA. & Craik, D.J. (1995) Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata. Biochemistry 34, 14304-14311.
- Neurath, H. (1984) Evolution of proteolytic enzymes. Science 224, 350-357.
- Onesti, S., Brick, P. & Blow, D.M. (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. J. Mol Biol 217, 153-176.
- Osmark, P., Sorensen, P. & Poulsen, F.M. (1993) Context dependent of protein secondary structure formation: The three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin Carlsberg. Biochemistry 32, 11007-11014.
- Otlewski, J. & Zbyryt, T. (1994) Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. I. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine /^-trypsin. Biochemistry 33, 200-207.
- Otlewski, J., Zbyryt, T., Dryjanski, M., Bulaj, G. & Wilusz, T. (1994) Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. II. Limited proteolysis of Cucurbita maxima trypsin inhibitor I (CMTI I) by pepsin. Biochemistry 33, 208-213.
- Pal, G.P., Kavounis, C.A., Jany, K.D. & Tserno- glou, D. (1994) The three-dimensional structure of the complex of proteinase K with its naturally occurring inhibitor. FEBS Lett. 341, 167-170.
- Peng. J.W. & Wagner, G. (1992) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31, 8571-8586.
- Pereira, P.J., Bergner, A., Macedo-Riberio, S., Huber, R., Matschiaer, G., Fritz, H., Sommer- hoff, C.P. & Bode, W. (1998) Human beta-tryptase is aring-like treatment with active sites facing a central pore. Nature 392, 306-311.
- Perona, J.J., Tsu, C.A., Fletterick, R.J. & Craik, C.S. (1993) Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J. MoL BiolI 230, 919-933.
- Perona, J.J., Tsu, C.A., Craik, C.S. & Fletterick, R.J. (1997) Crystal structure of an ecotin- col- lagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry 36, 5381-5392.
- Polanowska, J., Krokoszynska, I., Czapinska, H., Watorek, W., Dadlez, M. & Otiewski, J. (1998) Specificity of human cathepsin G. Biochim. Biophys. Acta 1386, 189-198.
- Potempa, J., Korzus, E. & Travis, J. (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol Chem. 269. 15957-15960.
- Priestle, J.P. & Di Marco, S. (1997) Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LD- TI-tryptase system. Structure 5, 1465-1474.
- Qasim, M.A., Ranjbar, M.R., Wynn, R., Anderson, S. & Laskowski, M., Jr. (1995) Ionizable Pi residues in serine proteinase inhibitors undergo large pK shifts on complex formation. J. Biol Chem. 270, 1-4.
- Qasim, M.A., Ganz, P.J., Saunders, C.W., Bate- man, K.S., James, M.N.G. & Laskowski, M., Jr. (1997) Interscaffolding additivity. Association of Pi variants of eglin c and of turkey ovomucoid third domain with serine proteinases. Biochemistry 36, 1598-1607.
- Quast, U., Engel, J., Steffen, E., Tschesche, H. & Kupfer, S. (1978) Kinetics of the interaction of a-chymotryp8in with trypsin kallikrein inhibitor (Kuuitz) in which the reactive-site peptide bond Lys-15-Alal6 is split. Eur. J. Biochem. 86, 353-360.
- Read, R.J., Fujinaga, M., Sielecki, A.R. & James, M.N.G. (1983) Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 A resolution. Biochemistry 22,4420-4433.
- Roberts, B.L., Markland, W., Ley, A.C., Kent, R.B., White, D.W., Guterman, S.K. & Ladner, R.C. (1992) Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phages. Proc. Natl Acad Sci. U.S.A. 89, 2429-2433.
- Rydel, T.J., Ravichandran, K.G., Tulinsky, A., Bode, W., Huber, R., Roitsch, C. & Fenton, J.W. (1990) The structure of a complex of recombinant hirudin and human a-thrombin. Science 249, 277-280.
- Rydel, T.J., Tulinsky, A., Bode, W. & Huber, R. (1991) Refined structure of the hirudin- thrombin complex. J. Mol Biol. 221,583-601.
- Ryu, S.-E., Choi, H.-J., Kwon, K.-S., Lee, K.N. & Yu, M.-H. (1996) The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: Crystal structure of an uncleaved aj-antitrypsin at 2.7 A. Structure 4, 1181-1192.
- Schechter, I. & Berger, A. (1967) On the size of the active site in proteases. Biochem Biophys. Res. Commun. 27, 157-162.
- Scheidig, A.J., Hynes, T.R., Pelletier, L.A., Wells, J.A. & Kossiakoff, A.A. (1997) Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid ^-precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities. Protein Sci 6, 1806-1824.
- Schreuder, H.A., de Boer, B., Dijkema, R., Mulders, J., Theunissen, H.J.M., Grootenhuis, P.DJ. & Hoi, W.G.J. (1994) The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nature Struct Biol 1, 48-54.
- Schulze, A.J., Baumann, U., Knof, S., Jaeger, E., Huber. R. & Laurell, C.B. (1990) Structural transition of alpha l-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur. J. Biochem. 194, 51-56.
- Seeram, S.S., Hiraga, K. & Oda, K. (1997) Peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor. J. Biochem. (Tokyo) 122, 788-794.
- Sharp, A.M., Stein, P.E., Pannu, N.S., Carrell, R.W., Berkenpas, M.B., Ginsburg, D., Lawrence, D.A. & Read, R.J. (1999) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Stricture 7, 111-118.
- Shaw, G.L., Davis, B., Keeler, J. & Fersht, A.R. (1995) Backbone dynamics of chymotrypsin inhibitor 2: Effect of breaking the active site bond and its implications for the mechanism of inhibition of serine proteases. Biochemistry 34, 2225-2233.
- Shin, D.H., Song, H.K., Seong, I.S., Lee, C.S., Chung, C.H. & Suh, S.W. (1996) Crystal structure analyses of uncomplexed ecotin in two crystal forms: Implications for its function and stability. Protein Sci. 5, 2236-2247.
- Shore, J.D., Day, D.E., Francis-Chmura, A.M., Verhamme, I., Kvasman, J., Lawrence, D.A. & Ginsburg, D. (1995) A fluorescent probe of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J. Biol Chem. 270, 5395-5398.
- Siekmann, J., Wenzel, H.R., Matuszak, E., von Goldammer, E. & Tschesche, H. (1988) The pH dependence of the equilibrium constant K^a for the hydrolysis of the Lys -Ala reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin). J. Prot Chem. 7, 633-640.
- Skinner, R., Abrahams, J.-P., Whisstock, J.C., Lesk, A.M., Carrell, R.W. & Wardell, M.R. (1997) The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site. J. MoL Biol. 266, 601-609.
- Skinner, R., Chang, W.S.W., Jin, L., Pei, X., Huntington, J.A., Abrahams, J.P., Carrell, R.W. & Lomas, D.A. (1998) Implications for function and therapy of a 2.9 A structure of binary- complexed antithrombin. J. MoL BioL 283, 9-14.
- Song, H.K. & Suh, S.W. (1998) Kunitz-type soybean trypsin inhibitor revisited: Refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J. MoL BioL 275, 347-363.
- Stein, P.E., Tewkesbury, C. & Carrell, R.W. (1989) Ovalbumin and angiotensinogen lack serpin S-R conformational change. Biochem. J. 262, 103-107.
- Stein, P., Leslie, A.G.W., Finch, J.T., Turnell, W.G., McLaughlin, P.J. & Carrell, R.W. (1990) Crystal structure of ovalbumin as a model for the reactive center of serpins. Nature 347, 99-102.
- Stein, P., Leslie, A.G.W., Finch, J.T. & Carrell, R.W. (1991) Crystal structure of uncleaved ovalbumin at 1.95 A resolution. J. MoL BioL 221, 941-959.
- Stein, P.E. & Carrell, R.W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct BioL 2, 96-113.
- Stone, S.R., Whisstock, J.C., Bottomely, S.P. & Hopkins, P.C.R. (1997) Serpins. A mechanistic class of their own. Adv. Exp. Med. BioL 425, 5-15.
- Strobl, S., Miihlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockshuber, R. & Holak, T.A. (1995) Determination of the three-dimensional structure of the Afunctional a-amylase/ trypsin inhibitor from ragi seeds by NMR spectroscopy. Biochemistry 34, 8281-8293.
- Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Riith, F.X. & Glockshuber, R. (1998) A novel strategy for inhibition of a-amylases: Yellow meal worm a-amylase in complex with the ragi bifunctional inhibitor at 2.5 A resolution. Structure 6, 911-921.
- Stubbs, M.T. & Bode, W. (1995) The clot thickens: Clues provided by thrombin structure. Trends Biochem. Sci. 20, 23-28.
- Stubbs, M.T., Morenweiser, R., Stiirzebecher, J., Bauer, M., Bode, W., Huber, R., Piechottka, G. P., Matschiner, G., Sommerhoff, C.P., Fritz, H. & Auerswald, E.A. (1997) The three<iimen- sional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. J. BioL Chem. 272, 19931-19937.
- Suzuki, A., Yamane, T., Ashida, T., Norioka, S., Hara, S. & Ikenaka, T. (1993) Crystallographic refinement of Bowman-Birk type proteases inhibitor A-II from peanut (Arackis hypogaea) at 2.3 A resolution. J. Mol Biol. 234, 722-734.
- Szyperski, T., Giintert, P., Stone, S.R. & Wuthrich, K. (1992a) Nuclear magnetic resonance solution structure of hirudin(l-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain. J. Mol. Biol. 228, 1193-1205.
- Szyperski, T., Giintert, P., Stone, S.R., Tulinsky, A., Bode, W., Huber, R. & Wuthrich, K. (1992b) Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin (1-51). J. Mol Biol 228, 1206-1211.
- Takeuchi, Y., Satow, Y., Nakamura, K.T. & Mitsui, Y. (1991) Refined crystal structure of the com plex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J. Mol Biol 221, 309-325.
- Takeuchi, Y., Nonaka, T., Nakamura, K.T., Kojima, S., Miura, K.-I. & Mitsui, Y. (1992) Crystal structure of an engineered subtilisin inhibitor complexed with bovine trypsin. Proc. Natl Acad. Sci U.S.A. 89, 4407-4411.
- Tamura, A., Kanaori, K., Kojima, S., Kumagai, I., Miura, K. & Akasaka, K. (1991) Mechanism of temporary inhibition in Streptomyces subtilisin inhibitor induced by an amino acid substitution, tryptophan 86 replaced by histidine. Biochemistry 30, 5275-5286.
- Travis, J. & Sdvesen, G.S. (1983) Human plasma proteinase inhibitors. Anna. Rev. Biochem. 52, 655-709.
- Tsunemi, M., Matsuura, Y., Sakakibara, S. & Katsube, Y. (1996) Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution. Biochemistry 35, 11570- 11576.
- Tsunogae, Y., Tanaka, I., Yamane, T., Kikkawa, J., Achida, J.T., Ishikawa, C., Watanabe, K., Nakamura, S. & Takahashi, K. (1986) Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin. J. Biochem (Tokyo) 100, 1637-1G4G.
- Tucker, H.M., Mottonen, J., Goldsmith, E.J. & Gerard, R.D. (1995) Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Nature Struct Biol 2, 442-445.
- Uson, I., Sheldrick, G.M., de La Fortelle, E., Bricogne, G., Di Marco, S., Priestle, J.P. & Grutter, M.G. (1999) The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged serine proteases. Structure 7, 55-63.
- Vallee, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K.W., Svensson, B. & Haser, R. (1998) Barley a-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 A resolution. Structure 6, 649-659.
- van de Locht, A., Lamba, D., Bauer, M., Huber, R., Friedrich, T., Kroger, B., Hoffken, W. & Bode, W. (1995) Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J. 14, 5149-5157.
- van de Locht, A., Stubbs, M.T., Bode, W., Friedrich, T., Bollschweiler, C., Hoffken, W. & Huber, R. (1996) The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J. 22, 6011-6017.
- van de Locht, A., Bode, W., Huber, R., Le Bonniec, B.F., Stone, S.R., Esmon, C.T. & Stubbs, M.T. (1997) The thrombin E192Q-BPTI complex reveals gross structural rearrangements for the interaction with antithrombin and thrombomodulin. EMBO J. 16, 2977-2984.
- Walkenhorst, W.F.. Krezel. A.M.. Rhyu. G.I. & Markley, J.L. (1994) Solution structure of reactive site hydrolyzed turkey ovomucoid third domain by nuclear magnetic resonance and distance geometry methods. J. Mol Biol 242, 215-230.
- Wardell, M.R., Abrahams, J.P., Bruce, D., Skinner, R. & Leslie, A.G. (1993) Crystallization and preliminary X-ray diffraction analysis of two conformations of intact human anti- thrombin. J. MoL BioL 234, 1253-1258.
- Waxman, L., Smith, D.E., Arcuri, K.E. & Vlasuk, G.P. (1990) Tick anticoagulant peptide (tap) is a novel inhibitor of blood coagulation factor Xa. Science 248, 593-596.
- Wei, A., Rubin, H., Cooperman, B.S. & Christ- ianson, D.W. (1994) Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nature Struct Biol. 1, 251-257.
- Wei, A., Alexander, R.S., Duke, J., Ross, H., Rosenfeld, S.A. & Chang, C.H. (1998) Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J. MoL BioL 283, 147-154.
- Wells, J.A. (1990) Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517.
- Werner, M.H. & Wemmer, D.E. (1992) Three-dimensional structure of soybean trypsin/chy- motrypsin Bowman-Birk inhibitor in solution. Biochemistry 31, 999-1010.
- Whisstock, J., Skinner, R. & Lesk, A.M. (1998) An atlas of serpin conformations. Trends Bio- chem. Sci. 23, 63-67.
- Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. (1984) Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J. MoL BioL 180, 301-329.
- Wright, H.T. & Scarsdale, J.N. (1995) Structural basis for serpin inhibitor activity. Proteins: Struct Funct Genet. 22, 210-225.
- Wright, H.T., Qian, H.Z. & Huber, R. (1990) Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. J. MoL BioL 213, 513-528.
- Xu, Y., Carr, P.D., Guss, J.M. & Ollis, D.L. (1998) The crystal structure of bikunin from the inter «-inhibitor complex: A serine protease inhibitor with two Kunitz domains. J. MoL BioL 276, 955-966.
- Yang, S.Q., Wang, C.-I., Gillmor, S.A., Fletterick, R.J. & Craik, C.S. (1998) Ecotin: A serine protease inhibitor with two distinct and interact ing binding sites. J. MoL BioL 279,945-957.
- Yu, M.-H., Weissman, J.S. & Kim, P.S. (1995) Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J. MoL BioL 249, 388-397.
- Zbyryt, T. & Otlewski, J. (1991) Interaction between squash inhibitors and bovine trypsi- nogen. Biol. Chem. Hoppe-Seyler 372, 255- 262.
- Zemke, K.J., Miiller-Farhnow, A., Jany, K.-D., Pal, G.P. & Saenger, W. (1991) The three-dimensional structure of the bifunctional proteinase K/a-amylase inhibitor from wheat (PKI3) at 2.5 A resolution. FEBS Lett 279, 240-242.
- Zhang, E., St Charles, R. & Tulinsky, A. (1999) Structure of extracellular tissue factor complexed with factor VI Ia inhibited with a BPTI mutant. J. MoL BioL 285, 2089-2104.
- Zweckstetter, M., Czisch, M., Mayer, U., Chu, M.-L., Zinth, W., Timpl, R. & Holak, T.A. (1995) Structure and multiple conformations of the Kunitz-type domain from human type VI collagen a3(VI) chain in solution. Structure 4, 195-209.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-8ae80520-d04d-4a70-a171-9ff5ac834fb5