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Receptory sprzężone z białkami G (GPCR) ; struktura i oddziaływania z bioligandami

Ciarkowski J., Czaplewski C., Kaźmierkiewicz R., Politowska E.

Wiadomości Chemiczne

1998

[Z] 52, 5-6

431-447

G protein-coupled receptors (GPCRs) from the largest superfamily, having over 1000 members, of integral membrane proteins sharing the following features: (i) All members from 7 hydrophobic a-helices of ~38 A (25 amino acids, 7 turns) along a single chain. The consecutive helices pass the membrane forth and back, starting from the extracellular side, to from a heptahelical transmembrane domain. This arrangement implicates 6 interhelical loops, whereof the even ones plus the N-terminus create the receptor's extracellular domain while the odd ones plus the C-terminus from its intracellular domain. (ii) All GPCRs are stimulated by extracellular signals of miscellaneous character. (iii) Stimulated GPCRs pass the extracellular signal via their transmembrane and intracellular domains to the cytosolic peripheral heterotrimeric GTP/GDP - binding proteins (G proteins), mediating the signal's further transduction to various cellular second messenger systems. A current status of structural studies on GPCRs, consisting of low ~7.5 A resolution experimental structures and supplementary molecular modelling, is presented. Subsequently, some results of author's own work on modelling essential interactions between the V2 vaasopressin renal receptor (V2R) and its agonists [Arg8] Vasopressin (AVP), [d-Arg8] Vasopressin (DAVP), and both the peptide desGly9 -[Mca1, D-Ile2, Ile4]AVP and the nonpeptide antagonist OPC-31260, are discussed. Finally perspectives for future developments are outlined.

Targets for majority of drugs: G protein-coupled receptors - their structure and interaction with bioligands

Ciarkowski J., Czaplewski C., Pasenkiewicz-Gierula M.

TASK Quarterly : scientific bulletin of Academic Computer Centre in Gdansk

1998

Vol. 2, No 4

583-599

G protein-coupled receptors (GPCRs) are the most frequent targets for many drugs. They form the largest superfamily of integral membrane proteins, of which more than 1000 members have the following common features: (i) All GPCRs form 7 hydrophobic a-helices of length ~38A (25 amino acids, 7 turns) along a single chain. The consecutive helices alternatively cross the membrane, starting from the extracellular side, so that they form a heptahelical transmembrane domain interwoven with 6 loops, of which the even ones plus the N-terminus create the receptor's extracellular domain while the odd ones plus the C-terminus form its intracellular domain. (ii) All GPCRs are stimulated by diverse extracellular (primary) signals. (iii) Stimulated GPCRs convey the primary signals via their transmembrane and intracellular domains to the cytosolic peripheral heterotrimeric GTP-binding proteins (G proteins), mediating the signal's further transduction to various cellular second messenger systems. A current status of structural studies on GPCRs, consisting of low ~7.5A resolution experimental structures and supplementary molecular modeling, is outlined. Subsequently, some results of authors' own work on studying essential interactions of the V2 vasopressin renal receptor (V2R) with its agonist [Arg8]Vasopressin (AVP) and selected antagonists are presented, as well as their possible impact on the biological signal transduction is discussed. Finally, perspectives for future developments are sketched.