1gcp

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|RELATEDENTRY=[[1gcq|1GCQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcp OCA], [http://www.ebi.ac.uk/pdbsum/1gcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gcp RCSB]</span>
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[[Category: Nishida, M.]]
[[Category: Nishida, M.]]
[[Category: Ogura, K.]]
[[Category: Ogura, K.]]
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[[Category: sh3 domain]]
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[[Category: sh3 domain,vav]]
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[[Category: vav]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:26 2008''

Revision as of 17:41, 30 March 2008


PDB ID 1gcp

Drag the structure with the mouse to rotate
, resolution 2.1Å
Related: 1GCQ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF VAV SH3 DOMAIN


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.

About this Structure

1GCP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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