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Crystal structure of the multifunctional Gbeta5-RGS9 complex.

ABSTRACT: Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (Galpha) 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 beta5 (Gbeta5) subunit through an internal G protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the 1.95-A crystal structure of the Gbeta5-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.

SUBMITTER: Cheever ML

PROVIDER: S-EPMC2702320 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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Crystal structure of the multifunctional Gbeta5-RGS9 complex.

Cheever Matthew L ML Snyder Jason T JT Gershburg Svetlana S Siderovski David P DP Harden T Kendall TK Sondek John J

Nature structural & molecular biology 20080120 2

Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (Galpha) 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 beta5 (Gbeta5) subunit through an internal G protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the 1.95-A crystal structure of the Gbeta5-RGS9 complex, which is essential for ...[more]

PMID: 18204463

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