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| | <StructureSection load='2dw2' size='340' side='right'caption='[[2dw2]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2dw2' size='340' side='right'caption='[[2dw2]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dw2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DW2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DW2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dw0|2dw0]], [[2dw1|2dw1]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dw0|2dw0]], [[2dw1|2dw1]]</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=2dw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dw2 OCA], [http://pdbe.org/2dw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2dw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dw2 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=2dw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dw2 OCA], [https://pdbe.org/2dw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dw2 RCSB], [https://www.ebi.ac.uk/pdbsum/2dw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dw2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VM3VB_CROAT VM3VB_CROAT]] Zinc metalloproteinase-disintegrin-like VAP2B: zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. | + | [[https://www.uniprot.org/uniprot/VM3VB_CROAT VM3VB_CROAT]] Zinc metalloproteinase-disintegrin-like VAP2B: zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
2dw2 is a 2 chain structure with sequence from Crotalus atrox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Related: | |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[VM3VB_CROAT] Zinc metalloproteinase-disintegrin-like VAP2B: zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation.
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
Catrocollastatin/vascular apoptosis-inducing protein (VAP)2B is a metalloproteinase from Crotalus atrox venom, possessing metalloproteinase/disintegrin/cysteine-rich (MDC) domains that bear the typical domain architecture of a disintegrin and metalloproteinase (ADAM)/adamalysin/reprolysin family proteins. Here we describe crystal structures of catrocollastatin/VAP2B in three different crystal forms, representing the first reported crystal structures of a member of the monomeric class of this family of proteins. The overall structures show good agreement with both monomers of atypical homodimeric VAP1. Comparison of the six catrocollastatin/VAP2B monomer structures and the structures of VAP1 reveals a dynamic, modular architecture that may be important for the functions of ADAM/adamalysin/reprolysin family proteins.
Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins.,Igarashi T, Araki S, Mori H, Takeda S FEBS Lett. 2007 May 29;581(13):2416-22. Epub 2007 Apr 30. PMID:17485084[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Igarashi T, Araki S, Mori H, Takeda S. Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins. FEBS Lett. 2007 May 29;581(13):2416-22. Epub 2007 Apr 30. PMID:17485084 doi:10.1016/j.febslet.2007.04.057
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