 |
PDBsum entry 1gp2
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Complex (gtp-binding/transducer)
|
PDB id
|
|
|
|
1gp2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
344 a.a.
|
 |
|
|
|
|
|
|
|
339 a.a.
|
 |
|
|
|
|
|
|
|
54 a.a.
|
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
The structure of the g protein heterotrimer gi alpha 1 beta 1 gamma 2.
|
 |
|
Authors
|
 |
M.A.Wall,
D.E.Coleman,
E.Lee,
J.A.Iñiguez-Lluhi,
B.A.Posner,
A.G.Gilman,
S.R.Sprang.
|
 |
|
Ref.
|
 |
Cell, 1995,
83,
1047-1058.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |