1. Crystal structure of the multifunctional Gbeta5-RGS9 complex.
- Author
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Cheever ML, Snyder JT, Gershburg S, Siderovski DP, Harden TK, and Sondek J
- Subjects
- Binding Sites, Crystallography, X-Ray, Dimerization, Humans, Models, Molecular, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, GTP-Binding Protein beta Subunits chemistry, RGS Proteins chemistry
- 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.
- Published
- 2008
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