Crystal structure of the multifunctional Gβ5-RGS9 complex

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

doi:10.1038/nsmb.1377

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 journal › Article › peer-review

86 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 language	English
Pages (from-to)	155-162
Number of pages	8
Journal	Nature Structural and Molecular Biology
Volume	15
Issue number	2
DOIs	https://doi.org/10.1038/nsmb.1377
State	Published - Feb 2008

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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-{\AA} 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.",

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AU - Cheever, Matthew L.

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AU - Siderovski, David P.

AU - Harden, T. Kendall

AU - Sondek, John

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AB - 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.

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Crystal structure of the multifunctional Gβ5-RGS9 complex

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