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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.