Crystal structure of the multifunctional Gβ5-RGS9 complex

Matthew L. Cheever, Jason T. Snyder, Svetlana Gershburg, David P. Siderovski, T. Kendall Harden, John Sondek

Research output: Contribution to journalArticle

76 Scopus citations

Abstract

Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein α (Gα) 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 β5 (Gβ5) subunit through an internal G protein γ (Gγ)-subunit-like (GGL) domain. Here we present the 1.95-Å crystal structure of the Gβ5-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.

Original languageEnglish
Pages (from-to)155-162
Number of pages8
JournalNature Structural and Molecular Biology
Volume15
Issue number2
DOIs
StatePublished - Feb 2008

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    Cheever, M. L., Snyder, J. T., Gershburg, S., Siderovski, D. P., Harden, T. K., & Sondek, J. (2008). Crystal structure of the multifunctional Gβ5-RGS9 complex. Nature Structural and Molecular Biology, 15(2), 155-162. https://doi.org/10.1038/nsmb.1377