User:Olivier Laprevote/Sandbox 1

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[[Image:Vav_domains_-_Copie.png]]
[[Image:Vav_domains_-_Copie.png]]
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The Vav1 <scene name='75/751211/Structure_vav/3'>structural domains</scene> are (from N ter to C ter): a '''calponin-homology''' (CH) domain, an '''acidic''' (Ac) domain, a '''DBL-homology''' (DH) domain also known as a '''rhoGEF''' domain, a '''pleckstrin-homology''' (PH) domain, a '''phorbol esters/diacylglycerol binding''' (C1) domain and '''Src-homology''' (SH) 3 and 2 domains. <ref>http://smart.embl.de/smart/show_motifs.pl?GENOMIC=1&DO_PFAM=DO_PFAM&INCLUDE_SIGNALP=INCLUDE_SIGNALP&ID=9606.ENSP00000472929</ref>
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The Vav1 <scene name='75/751211/Structure_vav/3'>structural domains</scene> are (from N ter to C ter): a '''calponin-homology''' (CH) domain, an '''acidic''' (Ac) domain, a '''DBL-homology''' (DH) domain also known as a '''rhoGEF''' domain, a '''pleckstrin-homology''' (PH) domain, a '''phorbol esters/diacylglycerol binding''' (C1) domain and '''Src-homology''' (SH) 3 and 2 domains. <ref>http://smart.embl.de/smart/show_motifs.pl?GENOMIC=1&DO_PFAM=DO_PFAM&INCLUDE_SIGNALP=INCLUDE_SIGNALP&ID=9606.ENSP00000472929</ref> <ref>PMID:20141838 </ref>
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<scene name='75/751211/Ch_domain/1'>Calponin-homology (CH) domain</scene> : When the CH domain is deleted, Vav has a phosphorylation-independant GEF activity. Studies on Vav3 implies that CH plays a role in inhibition via its interactions with the <scene name='75/751211/Ch_and_ac/1'>Ac</scene> (between the residue 49 in CH and 181 in Ac), DH and <scene name='75/751211/Ch_and_c1/1'>C1</scene> regions (C1 interacts with L101 and L104 of CH). The contacts with DH and C1 seem passively driven by the interactions between Ac and CH, though. <ref>PMID:15775967</ref>
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<scene name='75/751211/Ch_domain/1'>Calponin-homology (CH) domain</scene> (residues 1 - 119): When the CH domain is deleted, Vav has a phosphorylation-independant GEF activity. Studies on Vav3 implies that CH plays a role in inhibition via its interactions with the <scene name='75/751211/Ch_and_ac/1'>Ac</scene> (between the residue 49 in CH and 181 in Ac), DH and <scene name='75/751211/Ch_and_c1/1'>C1</scene> regions (C1 interacts with L101 and L104 of CH). The contacts with DH and C1 seem passively driven by the interactions between Ac and CH, though. <ref>PMID:15775967</ref>
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<scene name='75/751211/Ac_domain/1'>Acidic (Ac) domain</scene> (residues 134 - 187): contains the Tyrosine (Y174) which activates Vav activity when phosphorylated.
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<scene name='75/751211/Dh_domain/1'>DBL-homology (DH) domain</scene> (residues 194 - 373): present in every Rho/rac GEF, it is the active site of the GTP exchange with the C1 domain in Vav. It always has a PH domain at its C terminal.

Revision as of 11:02, 27 January 2017

Proto-oncogene vav

Caption for this structure

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ http://www.uniprot.org/uniprot/P15498#function
  4. ↑ http://smart.embl.de/smart/show_motifs.pl?GENOMIC=1&DO_PFAM=DO_PFAM&INCLUDE_SIGNALP=INCLUDE_SIGNALP&ID=9606.ENSP00000472929
  5. ↑ Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, Fernandez-Zapico ME, Billadeau DD, Machius M, Tomchick DR, Rosen MK. Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. Cell. 2010 Jan 22;140(2):246-56. PMID:20141838 doi:10.1016/j.cell.2009.12.033
  6. ↑ Llorca O, Arias-Palomo E, Zugaza JL, Bustelo XR. Global conformational rearrangements during the activation of the GDP/GTP exchange factor Vav3. EMBO J. 2005 Apr 6;24(7):1330-40. Epub 2005 Mar 10. PMID:15775967 doi:http://dx.doi.org/10.1038/sj.emboj.7600617

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Olivier Laprevote

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