1f5x

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5x OCA], [http://www.ebi.ac.uk/pdbsum/1f5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f5x RCSB]</span>
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'''NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN'''
'''NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN'''
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[[Category: Rosen, M K.]]
[[Category: Rosen, M K.]]
[[Category: 11 alpha-helice]]
[[Category: 11 alpha-helice]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:56:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:33 2008''
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Revision as of 12:56, 2 May 2008

Image:1f5x.jpg

Template:STRUCTURE 1f5x

NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN


Overview

Rho-family GTPases transduce signals from receptors leading to changes in cell shape and motility, mitogenesis, and development. Proteins containing the Dbl homology (DH) domain are responsible for activating Rho GTPases by catalyzing the exchange of GDP for GTP. Receptor-initiated stimulation of Dbl protein Vav exchange activity involves tyrosine phosphorylation. We show through structure determination that the mVav1 DH domain is autoinhibited by an N-terminal extension, which lies in the GTPase interaction site. This extension contains the Tyr174 Src-family kinase recognition site, and phosphorylation or truncation of this peptide results in stimulation of GEF activity. NMR spectroscopy data show that the N-terminal peptide is released from the DH domain and becomes unstructured upon phosphorylation. Thus, tyrosine phosphorylation relieves autoinhibition by exposing the GTPase interaction surface of the DH domain, which is obligatory for Vav activation.

About this Structure

1F5X is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation., Aghazadeh B, Lowry WE, Huang XY, Rosen MK, Cell. 2000 Sep 1;102(5):625-33. PMID:11007481 Page seeded by OCA on Fri May 2 15:56:31 2008

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