High-resolution structure of RGS17 suggests a role for Ca²⁺ in promoting the GTPase-activating protein activity by RZ subfamily members.

ABSTRACT: Regulator of G protein signaling (RGS) proteins are negative regulators of G protein-coupled receptor (GPCR) signaling through their ability to act as GTPase-activating proteins (GAPs) for activated Gα subunits. Members of the RZ subfamily of RGS proteins bind to activated Gα_o, Gα_z, and Gα_i1-3 proteins in the nervous system and thereby inhibit downstream pathways, including those involved in Ca²⁺-dependent signaling. In contrast to other RGS proteins, little is known about RZ subfamily structure and regulation. Herein, we present the 1.5-Å crystal structure of RGS17, the most complete and highest-resolution structure of an RZ subfamily member to date. RGS17 cocrystallized with Ca²⁺ bound to conserved positions on the predicted Gα-bindi

SUBMITTER: Sieng M 

PROVIDER: S-EPMC6527179 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature