Structural insights into G-protein-coupled receptor activation

被引：75

作者：

Weis, William I. ^{[1
,2
]}

Kobilka, Brian K. ^{[1
,3
]}

机构：

[1] Stanford Univ, Dept Cellular & Mol Physiol, Sch Med, Stanford, CA 94305 USA

[2] Stanford Univ, Dept Biol Struct, Sch Med, Stanford, CA 94305 USA

[3] Stanford Univ, Dept Med, Sch Med, Stanford, CA 94305 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2008年 / 18卷 / 06期

关键词：

D O I：

10.1016/j.sbi.2008.09.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

G-protein-coupled receptors (GPCRs) are the largest family of eukaryotic plasma membrane receptors, and are responsible for the majority of cellular responses to external signals. GPCRs share a common architecture comprising seven transmembrane (TM) helices. Binding of an activating ligand enables the receptor to catalyze the exchange of GTP for GDP in a heterotrimeric G protein. GPCRs are in a conformational equilibrium between inactive and activating states. Crystallographic and spectroscopic studies of the visual pigment rhodopsin and two beta-adrenergic receptors have defined some of the conformational changes associated with activation.

引用

页码：734 / 740

页数：7

共 32 条

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