Crystal structure of the multifunctional Gβ5-RGS9 complex

被引：86

作者：

Cheever, Matthew L. ^{[1
,2
]}

Snyder, Jason T. ^{[1
]}

Gershburg, Svetlana ^{[1
]}

Siderovski, David P. ^{[1
,3
]}

Harden, T. Kendall ^{[1
,2
]}

Sondek, John ^{[1
,2
,4
]}

机构：

[1] Univ N Carolina, Sch Med, Dept Pharmacol, Chapel Hill, NC 27599 USA

[2] Univ N Carolina, Sch Med, Ctr Comprehens Canc, Chapel Hill, NC 27599 USA

[3] Univ N Carolina, Sch Med, UNC Neurosci Ctr, Chapel Hill, NC 27599 USA

[4] Univ N Carolina, Sch Med, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 02期

关键词：

D O I：

10.1038/nsmb.1377

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：

Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (G alpha) subunits and are vital for proper signaling kinetics downstream of G protein-coupled receptors (GPCRs). R7 subfamily RGS proteins specifically and obligately dimerize with the atypical G protein beta 5 (G beta 5) subunit through an internal G protein gamma (G gamma)-subunit-like (GGL) domain. Here we present the 1.95-angstrom crystal structure of the G beta 5-RGS9 complex, which is essential for normal visual and neuronal signal transduction. This structure reveals a canonical RGS domain that is functionally integrated within a molecular complex that is poised for integration of multiple steps during G-protein activation and deactivation.

引用

页码：155 / 162

页数：8

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