1GP2

G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND

1GP2 の概要

• エントリーDOI: 10.2210/pdb1gp2/pdb
• 分子名称: G PROTEIN GI ALPHA 1, G PROTEIN GI BETA 1, G PROTEIN GI GAMMA 2, ... (5 entities in total)
• 機能のキーワード: signal transduction protein, gtpase, wd40, ras-like, complex (gtp-binding-transducer), complex (gtp-binding-transducer) complex, complex (gtp-binding/transducer)
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Nucleus: P10824; Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P63212
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 85973.04

構造登録者

Wall, M.A.,Sprang, S.R. (登録日: 1996-11-13, 公開日: 1997-02-12, 最終更新日: 2024-02-07)

主引用文献

Wall, M.A.,Coleman, D.E.,Lee, E.,Iniguez-Lluhi, J.A.,Posner, B.A.,Gilman, A.G.,Sprang, S.R.
The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.
Cell(Cambridge,Mass.), 83:1047-1058, 1995

PubMed 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.

PubMed: 8521505
DOI: 10.1016/0092-8674(95)90220-1

実験手法

X-RAY DIFFRACTION (2.3 Å)