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- Title
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
- Authors
Cheever, Matthew L; Snyder, Jason T; Gershburg, Svetlana; Siderovski, David P; Harden, T Kendall; Sondek, John
- 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.
- Publication
Nature structural & molecular biology, 2008, Vol 15, Issue 2, p155
- ISSN
1545-9985
- Publication type
Journal Article
- DOI
10.1038/nsmb.1377