1agr
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COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4
OverviewOverview
RGS proteins are GTPase activators for heterotrimeric G proteins. We, report here the 2.8 A resolution crystal structure of the RGS protein RGS4, complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is, visible in the crystal. The core domain binds to the three switch regions, of G(i alpha1), but does not contribute catalytic residues that directly, interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze, rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i, alpha1), although the conserved Asn-128 from RGS4 could also play a, catalytic role by interacting with the hydrolytic water molecule or the, side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also, consistent with the activity of RGS proteins as antagonists of G(alpha), effectors.
About this StructureAbout this Structure
1AGR is a Protein complex structure of sequences from Rattus norvegicus with MG, ALF, GDP and CIT as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis., Tesmer JJ, Berman DM, Gilman AG, Sprang SR, Cell. 1997 Apr 18;89(2):251-61. PMID:9108480
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