1wq8

<StructureSection load='1wq8' size='340' side='right' caption='[[1wq8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1wq8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspic_viper Aspic viper]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WQ8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wq9|1wq9]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wq8 OCA], [http://pdbe.org/1wq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wq8 RCSB], [http://www.ebi.ac.uk/pdbsum/1wq8 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/TXVE_VIPAP TXVE_VIPAP]] Induces angiogenesis, probably through VEGF receptor (VEGFR) signaling, as well as drastic hypotension. The hypotension is mediated by nitric oxide, which is produced by VEGF-activated endothelium NO synthase. Increases capillary permeability when injected intradermally into rat.<ref>PMID:10512636</ref> <ref>PMID:14600159</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wq/1wq8_consurf.spt"</scriptWhenChecked>

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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>

*[[Vascular Endothelial Growth Factor|Vascular Endothelial Growth Factor]]

[[Category: Aspic viper]]

[[Category: Mizuno, H]]

[[Category: Morita, T]]

[[Category: Suto, K]]

[[Category: Yamazaki, Y]]

[[Category: Vegf-f]]