1r8q: Difference between revisions

Revision as of 09:17, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1r8q.png

Template:STRUCTURE 1r8q

FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAINFULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN

Template:ABSTRACT PUBMED 14654833

About this StructureAbout this Structure

1R8Q is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor., Renault L, Guibert B, Cherfils J, Nature. 2003 Dec 4;426(6966):525-30. PMID:14654833

Page seeded by OCA on Tue Jul 29 09:17:30 2008

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OCA

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-'''FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN'''
+===FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN===
-==Overview==
+<!--
-Small GTP-binding (G) proteins are activated by GDP/GTP nucleotide exchange stimulated by guanine nucleotide exchange factors (GEFs). Nucleotide dissociation from small G protein-GEF complexes involves transient GDP-bound intermediates whose structures have never been described. In the case of Arf proteins, small G proteins that regulate membrane traffic in eukaryotic cells, such intermediates can be trapped either by the natural inhibitor brefeldin A or by charge reversal at the catalytic glutamate of the Sec7 domain of their GEFs. Here we report the crystal structures of these intermediates that show that membrane recruitment of Arf and nucleotide dissociation are separate reactions stimulated by Sec7. The reactions proceed through sequential rotations of the Arf.GDP core towards the Sec7 catalytic site, and are blocked by interfacial binding of brefeldin A and unproductive stabilization of GDP by charge reversal. The structural characteristics of the reaction and its modes of inhibition reveal unexplored ways in which to inhibit the activation of small G proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_14654833}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14654833 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14654833}}
 ==About this Structure==
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 [[Category: Renault, L.]]
 [[Category: Protein transport/exchange factor]]
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