1gp2

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(New page: 200px<br /><applet load="1gp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gp2, resolution 2.3&Aring;" /> '''G PROTEIN HETEROTRIME...)
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[[Image:1gp2.gif|left|200px]]<br /><applet load="1gp2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gp2.gif|left|200px]]<br /><applet load="1gp2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gp2, resolution 2.3&Aring;" />
caption="1gp2, resolution 2.3&Aring;" />
'''G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND'''<br />
'''G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1GP2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP2 OCA].
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1GP2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP2 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Sprang, S.R.]]
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[[Category: Sprang, S R.]]
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[[Category: Wall, M.A.]]
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[[Category: Wall, M A.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: complex (gtp-binding/transducer)]]
[[Category: complex (gtp-binding/transducer)]]
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[[Category: wd40]]
[[Category: wd40]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:12:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:26 2008''

Revision as of 10:52, 21 February 2008


1gp2, resolution 2.3Å

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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 with as ligand. 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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