View source for 1wq8


==Crystal structure of Vammin, a VEGF-F from a snake venom==
<StructureSection load='1wq8' size='340' side='right'caption='[[1wq8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wq8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vipera_aspis_aspis Vipera aspis aspis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WQ8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1wq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wq8 OCA], [https://pdbe.org/1wq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wq8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wq8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TXVE_VIPAA TXVE_VIPAA] Snake venom VEGFs may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase (PubMed:14600159). Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling (PubMed:14600159). May also induce capillary permeability through VEGF receptor (KDR/VEGFR-2) signaling.<ref>PMID:14600159</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wq/1wq8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wq8 ConSurf].
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== Publication Abstract from PubMed ==
Vascular endothelial growth factor-A (VEGF-A(165)) exerts multiple effects upon binding to the fms-like tyrosine kinase-1 (Flt-1) and the kinase insert domain-containing receptor (KDR). We recently identified two novel snake venom VEGFs (vammin and VR-1) having unique properties. These VEGFs, designated VEGF-Fs, are highly specific ligands for the kinase insert domain-containing receptor and exhibit potent biological activity both in vitro and in vivo when compared with VEGF-A(165). Here, we solved the crystal structures of vammin and VR-1 at 1.9 and 2.0 A resolutions, respectively. Both structures are very similar to each other, and these structures exhibit similar but significantly different features from the known structures of other VEGFs. These differences include a conformational difference in receptor-binding loop 3 caused by an amino acid residue insertion and a difference in surface potential on the possible binding surface for domain 3 of the receptor. These structural differences may be related to the highly selective ligand properties of VEGF-F.

Crystal structures of novel vascular endothelial growth factors (VEGF) from snake venoms: insight into selective VEGF binding to kinase insert domain-containing receptor but not to fms-like tyrosine kinase-1.,Suto K, Yamazaki Y, Morita T, Mizuno H J Biol Chem. 2005 Jan 21;280(3):2126-31. Epub 2004 Nov 12. PMID:15542594<ref>PMID:15542594</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1wq8" style="background-color:#fffaf0;"></div>

==See Also==
*[[VEGF 3D Structures|VEGF 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vipera aspis aspis]]
[[Category: Mizuno H]]
[[Category: Morita T]]
[[Category: Suto K]]
[[Category: Yamazaki Y]]