1f5x
From Proteopedia
(New page: 200px<br /><applet load="1f5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5x" /> '''NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL ...) |
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| - | [[Image:1f5x.jpg|left|200px]]<br /><applet load="1f5x" size=" | + | [[Image:1f5x.jpg|left|200px]]<br /><applet load="1f5x" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN'''<br /> | '''NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rho-family GTPases transduce signals from receptors leading to changes in | + | 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== | ==About this Structure== | ||
| - | 1F5X 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:// | + | 1F5X 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=1F5X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aghazadeh, B.]] | [[Category: Aghazadeh, B.]] | ||
| - | [[Category: Huang, X | + | [[Category: Huang, X Y.]] |
| - | [[Category: Lowry, W | + | [[Category: Lowry, W E.]] |
| - | [[Category: Rosen, M | + | [[Category: Rosen, M K.]] |
[[Category: 11 alpha-helices]] | [[Category: 11 alpha-helices]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:22 2008'' |
Revision as of 10:35, 21 February 2008
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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
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