1gcp

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[[Image:1gcp.jpg|left|200px]]<br /><applet load="1gcp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gcp.jpg|left|200px]]
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caption="1gcp, resolution 2.1&Aring;" />
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'''CRYSTAL STRUCTURE OF VAV SH3 DOMAIN'''<br />
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{{Structure
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|PDB= 1gcp |SIZE=350|CAPTION= <scene name='initialview01'>1gcp</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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'''CRYSTAL STRUCTURE OF VAV SH3 DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCP OCA].
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1GCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCP OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11406576 11406576]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11406576 11406576]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: vav]]
[[Category: vav]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:23 2008''

Revision as of 09:21, 20 March 2008

Image:1gcp.jpg


PDB ID 1gcp

Drag the structure with the mouse to rotate
, resolution 2.1Å
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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