PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
Czasopismo
2014 | 1 | 1 |
Tytuł artykułu

Conformational disorder in phosphopeptides: solution studies by CD and NMR techniques

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
In the last few years intrinsically disordered proteins (IDPs) have received great attention from the scientific community as they participate in several important biological processes and diseases. The intrinsic disorder and flexibility of IDPs grant them a number of advantages with respect to ordered proteins, such as conformational plasticity to bind several targets, a large interaction surface, involvement in high specificity/low affinity interactions, enhanced binding kinetics. It is assumed that post-translational modifications such as phosphorylation can stimulate structural rearrangement in IDPs and facilitate their binding to partners. To better understand at a structural level the multifaceted mechanisms that govern molecular recognition processes involving IDPs, we designed, synthesized by solid phase methods, and structurally characterized unstructured peptides. These molecules contain a putative disordered module, flanked at either the N- or C-terminal ends by a different phosphorylated amino acid (serine or threonine) to mimick the effects of phosphorylation. The absence of an ordered state in the designed peptides was proved experimentally by CD and NMR conformational studies that were carried out under different solution conditions
Wydawca

Czasopismo
Rocznik
Tom
1
Numer
1
Opis fizyczny
Daty
wydano
2014-01-01
online
2014-07-02
Twórcy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy
  • University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy
  • CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse - UMR 7282, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France
  • Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy/ Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy, filrossi@unina.it
Bibliografia
  • [1] V. N. Uversky, Int J Biochem Cell Biol 2011, 43, 1090-1103.
  • [2] M. M. Babu, Mol Biosyst 2012, 8, 21.[PubMed]
  • [3] J. J. Ward, J. S. Sodhi, L. J. McGuffin, B. F. Buxton, D. T. Jones, J Mol Biol 2004, 337, 635-645.
  • [4] Y. Cheng, T. LeGall, C. J. Oldfield, A. K. Dunker, V. N. Uversky, Biochemistry 2006, 45, 10448-10460.
  • [5] M. M. Babu, R. van der Lee, N. S. de Groot, J. Gsponer, Curr Opin Struct Biol 2011, 21, 432-440.[Crossref]
  • [6] V. N. Uversky, Expert Rev Proteomics 2010, 7, 543-564.[PubMed]
  • [7] G. P. Singh, D. Dash, Proteins 2007, 68, 602-605.
  • [8] A. B. Sigalov, Adv Exp Med Biol 2008, 640, 268-311.
  • [9] A. B. Sigalov, Mol Biosyst 2010, 6, 451-461.[PubMed]
  • [10] A. B. Sigalov, Self Nonself 2010, 1, 89-102.
  • [11] A. Accardo, A. Morisco, P. Palladino, R. Palumbo, D. Tesauro, G. Morelli, Mol Biosyst 2011, 7, 862-870.[PubMed]
  • [12] Y. Huang, Z. Liu, J Mol Biol 2009, 393, 1143-1159.
  • [13] B. A. Shoemaker, J. J. Portman, P. G. Wolynes, Proc Natl Acad Sci U S A 2000, 97, 8868-8873.
  • [14] P. Lieutaud, B. Canard, S. Longhi, BMC Genomics 2008, 9 Suppl 2, S25.
  • [15] W. Chang, P. D. White, Fmoc Solid Phase Peptide Synthesis. , Oxford University Press, New York, 2000.
  • [16] K. Wuthrich, NMR of Proteins and nucleic acids., John Wiley & Sons, New York, 1986.
  • [17] C. Griesinger, G. Otting, K. Wuthrich, R.R. Ernst, J Am Chem Soc 1988, 110, 7870-7872.
  • [18] U. Piantini, O.W. Sorensen, R.R. Ernst, J Am Chem Soc 1982, 104, 6800-6801.
  • [19] A. Kumar, R. R. Ernst, K. Wuthrich, Biochem Biophys Res Commun 1980, 95, 1-6.
  • [20] C. Dalvit, Journal of Biomolecular NMR 1998, 11, 437-444.
  • [21] C. Bartels, T. H. Xia, M. Billeter, P. Guntert, K. Wuthrich, J Biomol NMR 1995, 6, 1-10.[PubMed]
  • [22] T. Herrmann, P. Guntert, K. Wuthrich, J Mol Biol 2002, 319, 209-227.
  • [23] J. W. Craft, Jr., G. B. Legge, J Biomol NMR 2005, 33, 15-24.[PubMed]
  • [24] R. Koradi, M. Billeter, K. Wuthrich, J Mol Graph 1996, 14, 51-55, 29-32.[PubMed]
  • [25] J. F. Doreleijers, A. W. Sousa da Silva, E. Krieger, S. B. Nabuurs, C. A. Spronk, T. J. Stevens, W. F. Vranken, G. Vriend, G. W. Vuister, J Biomol NMR 2012, 54, 267-283.[Crossref]
  • [26] A. M. Fernandez-Escamilla, F. Rousseau, J. Schymkowitz , L. Serrano. Nat Biotechnol. 2004, 10, 1302-1306.
  • [27] M. Buck, Q Rev Biophys 1998, 31, 297-355.[PubMed]
  • [28] K. C. Hite, A. A. Kalashnikova, J. C. Hansen, Protein Sci 2012, 21, 531-538.[PubMed]
  • [29] B. Maestro, B. Galan, C. Alfonso, G. Rivas, M. A. Prieto, J. M. Sanz, PLoS One 2013, 8, e56904.
  • [30] V. L. Anderson, T. F. Ramlall, C. C. Rospigliosi, W. W. Webb, D. Eliezer, Proc Natl Acad Sci U S A 2010, 107, 18850-18855.
  • [31] D. S. Wishart, B. D. Sykes, F. M. Richards, J Mol Biol 1991, 222, 311-333.
  • [32] S. Ohnishi, K. Takano, Cell Mol Life Sci 2004, 61, 511-524.[PubMed]
  • [33] F. Rousseau, J. Schymkowitz, L. Serrano, Curr Opin Struct Biol 2006, 16, 118-126.[PubMed]
  • [34] M. von Bergen, P. Friedhoff, J. Biernat, J. Heberle, E. M. Mandelkow, E. Mandelkow, Proc Natl Acad Sci U S A 2000, 97, 5129-5134.
  • [35] M. R. Krebs, D. K. Wilkins, E. W. Chung, M. C. Pitkeathly, A. K. Chamberlain, J. Zurdo, C. V. Robinson, C. M. Dobson, J Mol Biol 2000, 300, 541-549.
  • [36] A. Thompson, A. R. White, C. McLean, C. L. Masters, R. Cappai, C. J. Barrow, J Neurosci Res 2000, 62, 293-301.[PubMed]
  • [37] J. Wang, Z. Cao, L. Zhao, S. Li, Int J Mol Sci 2011, 12, 3205-3219.[PubMed]
  • [38] H. Cui, M. J. Webber, S. I. Stupp, Biopolymers 2010, 94, 1-18.
  • [39] A. Accardo, G. Mangiapia, L. Paduano, G. Morelli, D. Tesauro, J Pept Sci 2013, 19, 190-197.[PubMed]
  • [40] C. Falciani, J. Brunetti, B. Lelli, A. Accardo, D. Tesauro, G. Morelli, L. Bracci, J Pept Sci 2013, 19, 198-204.[PubMed]
  • [41] A. Accardo, M. Leone, D. Tesauro, R. Aufiero, A. Benarouche, J. F. Cavalier, S. Longhi, F. Carriere, F. Rossi, Mol Biosyst 2013, 9, 1401-1410.[PubMed]
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_2478_ped-2014-0001
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.