View source for 2lnx


==Solution structure of Vav2 SH2 domain==
<StructureSection load='2lnx' size='340' side='right'caption='[[2lnx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lnx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnx OCA], [https://pdbe.org/2lnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnx RCSB], [https://www.ebi.ac.uk/pdbsum/2lnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VAV2_HUMAN VAV2_HUMAN] Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vav2 is a ubiquitous guanine nucleotide exchange factor (GEF) for the small GTPase Rac1. It regulates processes including cell migration, neuronal development and phagocytosis through interactions with different proteins. In this study, Arap3, a dual GTPase-activating protein (GAP) for RhoA and Arf6, was first identified to be a novel interaction partner for Vav2 both in vitro and in vivo. ITC and NMR chemical shift perturbation experiments demonstrated that Vav2 SH2 domain was able to interact directly with phosphorylated Y1403 and Y1408 within the C-terminal region of Arap3 with high affinities, with the dissociation constants (Kd) of approximately 0.27 and approximately 1.40muM, respectively. In addition, using different phosphotyrosine peptides, the pY +3 specificity of Vav2 SH2 domain was discovered. The solution structures of Vav2 SH2 domain in free and in complex with the phosphotyrosine peptide pY1408 were therefore determined to understand the structural basis of this recognition specificity. Structural analysis revealed that the presence of a Phe residue in the BG loop (BG6) leads to the formation of a shallow hydrophobic pY +3 pocket on the surface of Vav2 SH2 domain, which determines the pY +3 specificity of Vav2 SH2 domain.

Identification and structural basis for a novel interaction between Vav2 and Arap3.,Wu B, Wang F, Zhang J, Zhang Z, Qin L, Peng J, Li F, Liu J, Lu G, Gong Q, Yao X, Wu J, Shi Y J Struct Biol. 2012 Oct;180(1):84-95. doi: 10.1016/j.jsb.2012.06.011. Epub 2012, Jun 28. PMID:22750419<ref>PMID:22750419</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lnx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Shi Y]]
[[Category: Wu B]]
[[Category: Wu J]]
[[Category: Zhang J]]