1gp2

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp2 OCA], [http://www.ebi.ac.uk/pdbsum/1gp2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gp2 RCSB]</span>
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[[Category: Sprang, S R.]]
[[Category: Sprang, S R.]]
[[Category: Wall, M A.]]
[[Category: Wall, M A.]]
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[[Category: GDP]]
 
[[Category: complex (gtp-binding/transducer)]]
[[Category: complex (gtp-binding/transducer)]]
[[Category: gtpase]]
[[Category: gtpase]]
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[[Category: wd40]]
[[Category: wd40]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:29 2008''

Revision as of 17:48, 30 March 2008


PDB ID 1gp2

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND


Overview

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 Structure

1GP2 is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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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