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| | <StructureSection load='1wq8' size='340' side='right'caption='[[1wq8]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1wq8' size='340' side='right'caption='[[1wq8]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wq8]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WQ8 FirstGlance]. <br> | + | <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='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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wq9|1wq9]]</div></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wq8 ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Vascular Endothelial Growth Factor|Vascular Endothelial Growth Factor]] | + | *[[VEGF 3D Structures|VEGF 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Komori Y, Nikai T, Taniguchi K, Masuda K, Sugihara H. Vascular endothelial growth factor VEGF-like heparin-binding protein from the venom of Vipera aspis aspis (Aspic viper). Biochemistry. 1999 Sep 7;38(36):11796-803. PMID:10512636
- ↑ Yamazaki Y, Takani K, Atoda H, Morita T. Snake venom vascular endothelial growth factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2). J Biol Chem. 2003 Dec 26;278(52):51985-8. Epub 2003 Nov 4. PMID:14600159 doi:10.1074/jbc.C300454200
- ↑ Suto K, Yamazaki Y, Morita T, Mizuno H. 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. J Biol Chem. 2005 Jan 21;280(3):2126-31. Epub 2004 Nov 12. PMID:15542594 doi:10.1074/jbc.M411395200
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