|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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='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='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'>[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> |
| - | <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> | + | |
| | </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_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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 16: |
Line 15: |
| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wq/1wq8_consurf.spt"</scriptWhenChecked> | | <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/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 32: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Vascular Endothelial Growth Factor|Vascular Endothelial Growth Factor]] | + | *[[VEGF 3D Structures|VEGF 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 39: |
Line 38: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Vipera aspis aspis]] | | [[Category: Vipera aspis aspis]] |
| - | [[Category: Mizuno, H]] | + | [[Category: Mizuno H]] |
| - | [[Category: Morita, T]] | + | [[Category: Morita T]] |
| - | [[Category: Suto, K]] | + | [[Category: Suto K]] |
| - | [[Category: Yamazaki, Y]] | + | [[Category: Yamazaki Y]] |
| - | [[Category: Snake venom]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Vascular endothelial growth factor]]
| + | |
| - | [[Category: Vegf]]
| + | |
| - | [[Category: Vegf-f]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
|
