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The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.

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Affiliations

  • 1. Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235, USA.
      Authors
    • Wall MA 1
    (1 author)

ORCIDs linked to this article

Cell, 01 Dec 1995, 83(6):1047-1058
https://doi.org/10.1016/0092-8674(95)90220-1 PMID: 8521505 

Abstract 

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.

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