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 |
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Pages (from-to) | 155-162 |
Number of pages | 8 |
Journal | Nature Structural and Molecular Biology |
Volume | 15 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2008 |