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| | ==Structure of Bitistatin A== | | ==Structure of Bitistatin A== |
| - | <StructureSection load='2mop' size='340' side='right'caption='[[2mop]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''> | + | <StructureSection load='2mop' size='340' side='right'caption='[[2mop]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mop]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bitis_arietans Bitis arietans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2MOP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mop]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bitis_arietans Bitis arietans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOP FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2mop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mop OCA], [http://pdbe.org/2mop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mop RCSB], [http://www.ebi.ac.uk/pdbsum/2mop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mop ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 29 models</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=2mop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mop OCA], [https://pdbe.org/2mop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mop RCSB], [https://www.ebi.ac.uk/pdbsum/2mop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mop ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VM2_BITAR VM2_BITAR]] Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen.<ref>PMID:2600082</ref> | + | [https://www.uniprot.org/uniprot/VM2_BITAR VM2_BITAR] Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen.<ref>PMID:2600082</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Bitis arietans]] | | [[Category: Bitis arietans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Calvete, J]] | + | [[Category: Calvete J]] |
| - | [[Category: Carbajo, R J]] | + | [[Category: Carbajo RJ]] |
| - | [[Category: Perez, A]] | + | [[Category: Perez A]] |
| - | [[Category: Sanz, L]] | + | [[Category: Sanz L]] |
| - | [[Category: Bitis arietan]]
| + | |
| - | [[Category: Disintegrin]]
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| - | [[Category: Snake venom]]
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| - | [[Category: Toxin]]
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| Structural highlights
Function
VM2_BITAR Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen.[1]
Publication Abstract from PubMed
Extant disintegrins represent a family of polypeptides found in the venoms of Viperidae and Crotalidae snakes (vipers and rattlesnakes) that block potently and with high degree of selectivity the function of beta1 and beta3 integrin receptors. This toxin family owes its origin to the neofunctionalization of the extracellular region of an ADAM molecule recruited into the snake venom gland proteome in the Jurassic. The evolutionary structural diversification of the disintegrin scaffold, from the ancestral long disintegrins to the more recently evolved medium-sized, dimeric, and short disintegrins, involved the stepwise loss of pairs of class-specific disulfide linkages and the processing of the N-terminal region. NMR and crystal structures of medium-sized, dimeric, and short disintegrins have been solved. However, the structure of a long disintegrin was missing. The here reported NMR solution structures of two disulfide bond conformers of the long disintegrin bitistatin, from the African puff adder Bitis arietans, provide insights into how a structural domain of the extracellular region of an ADAM molecule recruited, and selectively expressed into the snake venom gland proteome as a PIII metalloprotease in the Jurassic has been since tranformed into a family of integrin receptor antagonists. This article is protected by copyright. All rights reserved.
NMR structure of bitistatin, a missing piece in the evolutionary pathway of snake venom disintegrins.,Carbajo RJ, Sanz L, Perez A, Calvete JJ FEBS J. 2014 Nov 1. doi: 10.1111/febs.13138. PMID:25363287[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shebuski RJ, Ramjit DR, Bencen GH, Polokoff MA. Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans. J Biol Chem. 1989 Dec 25;264(36):21550-6. PMID:2600082
- ↑ Carbajo RJ, Sanz L, Perez A, Calvete JJ. NMR structure of bitistatin, a missing piece in the evolutionary pathway of snake venom disintegrins. FEBS J. 2014 Nov 1. doi: 10.1111/febs.13138. PMID:25363287 doi:http://dx.doi.org/10.1111/febs.13138
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