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 journalArticlepeer-review

86 Scopus citations


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
Issue number2
StatePublished - Feb 2008


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