1gcq: Difference between revisions

Revision as of 05:07, 1 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:1gcq.png

Template:STRUCTURE 1gcq

CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINSCRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS

Template:ABSTRACT PUBMED 11406576

About this StructureAbout this Structure

1GCQ is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Novel recognition mode between Vav and Grb2 SH3 domains., Nishida M, Nagata K, Hachimori Y, Horiuchi M, Ogura K, Mandiyan V, Schlessinger J, Inagaki F, EMBO J. 2001 Jun 15;20(12):2995-3007. PMID:11406576

Page seeded by OCA on Tue Jul 1 05:06:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS'''
+===CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS===
-==Overview==
+<!--
-Vav is a guanine nucleotide exchange factor for the Rho/Rac family that is expressed exclusively in hematopoietic cells. Growth factor receptor-bound protein 2 (Grb2) has been proposed to play important roles in the membrane localization and activation of Vav through dimerization of its C-terminal Src-homology 3 (SH3) domain (GrbS) and the N-terminal SH3 domain of Vav (VavS). The crystal structure of VavS complexed with GrbS has been solved. VavS is distinct from other SH3 domain proteins in that its binding site for proline-rich peptides is blocked by its own RT loop. One of the ends of the VavS beta-barrel forms a concave hydrophobic surface. The GrbS components make a contiguous complementary interface with the VavS surface. The binding site of GrbS for VavS partially overlaps with the canonical binding site for proline-rich peptides, but is definitely different. Mutations at the interface caused a decrease in the binding affinity of VavS for GrbS by 4- to 40-fold. The structure reveals how GrbS discriminates VavS specifically from other signaling molecules without binding to the proline-rich motif.
+The line below this paragraph, {{ABSTRACT_PUBMED_11406576}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11406576 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11406576}}
 ==About this Structure==
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 [[Category: Protein-protein complex]]
 [[Category: Sh3 domain]]
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