1gg2
G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND
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OverviewOverview
The crystallographic structure of the G protein heterotrimer Gi alpha, 1(GDP)beta 1 gamma 2 (at 2.3 A) reveals two nonoverlapping regions of, contact between alpha and beta, an extended interface between beta and, nearly all of gamma, and limited interaction of alpha with gamma. The, major alpha/beta interface covers switch II of alpha, and GTP-induced, rearrangement of switch II causes subunit dissociation during signaling., Alterations in GDP binding in the heterotrimer (compared with alpha-GDP), explain stabilization of the inactive conformation of alpha by beta gamma., Repeated WD motifs in beta form a circularized sevenfold beta propeller., The conserved cores of these motifs are a scaffold for display of their, more variable linkers on the exterior face of each propeller blade.
About this StructureAbout this Structure
1GG2 is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus with GDP as ligand. The following page contains interesting information on the relation of 1GG2 with [G Proteins]. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2., Wall MA, Coleman DE, Lee E, Iniguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR, Cell. 1995 Dec 15;83(6):1047-58. PMID:8521505
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