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| {{STRUCTURE_1gcp| PDB=1gcp | SCENE= }} | | {{STRUCTURE_1gcp| PDB=1gcp | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF VAV SH3 DOMAIN'''
| | ===CRYSTAL STRUCTURE OF VAV SH3 DOMAIN=== |
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| ==Overview==
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| 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}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ogura, K.]] | | [[Category: Ogura, K.]] |
| [[Category: Sh3 domain,vav]] | | [[Category: Sh3 domain,vav]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:25:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:06:26 2008'' |
