Crystal structure of the multifunctional Gβ5–RGS9 complex
| Autor: | Svetlana Gershburg, John Sondek, T. Kendall Harden, David P. Siderovski, Jason Snyder, Matthew L. Cheever |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Binding Sites GTPase-activating protein G protein Neuronal signal transduction GTP-Binding Protein beta Subunits Biology Crystallography X-Ray Article Protein Structure Tertiary Cell biology G beta-gamma complex Structural Biology Heterotrimeric G protein RGS9 Humans sense organs Protein Structure Quaternary Dimerization Molecular Biology RGS Proteins Protein Binding G protein-coupled receptor |
| Zdroj: | Nature Structural & Molecular Biology. 15:155-162 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.1377 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|