@article{bdacdbd8a0a543b7be8ca5485fcae256,
title = "The structure of the G protein heterotrimer Giα1β1γ2",
abstract = "The crystallographic structure of the G protein heterotrimer Giα1(GDP)β1γ2 (at 2.3 A) reveals two nonoverlapping regions of contact between α and β, an extended interface between β and nearly all of γ, and limited interaction of α with γ. The major α/β interface covers switch II of α, and GTP-induced rearrangement of switch II causes subunit dissociation during signaling. Alterations in GDP binding in the heterotrimer (compared with α-GDP) explain stabilization of the inactive conformation of α by βγ. Repeated WD motifs in β form a circularized sevenfold β 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.",
author = "Wall, {Mark A.} and Coleman, {David E.} and Ethan Lee and I{\~n}iguez-Lluhi, {Jorge A.} and Posner, {Bruce A.} and Gilman, {Alfred G.} and Sprang, {Stephen R.}",
note = "Funding Information: Acknowledgments We are grateful to Albert Berghuis, Jim Naismith, and Ward Coates for assistance with data collection and processing; to Brian Sutton and Orelia Ortiz for assistance with illustrations; to Elliott M. Ross, Eva Neer, and Mark Mixon for helpful discussion; and to Marian Stanzel for skilled technical assistance. This work was supported by National Institutes of Health (NIH) grant DK46371 and Welch Foundation grant I-1229 to (S. R. S.) and by NIH grant GM34497, American Cancer Society grant BE30-0, Welch Foundation grant I-1 271, and the Raymond and Ellen Willie Chair of Molecular Neuropharmacology (to A. G. G.).",
year = "1995",
month = dec,
day = "15",
doi = "10.1016/0092-8674(95)90220-1",
language = "English",
volume = "83",
pages = "1047--1058",
journal = "Cell",
issn = "0092-8674",
publisher = "Elsevier B.V.",
number = "6",
}