View source for 2mop


==Structure of Bitistatin A==
<StructureSection load='2mop' size='340' side='right'caption='[[2mop]]' scene=''>
== Structural highlights ==
<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='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>
== Function ==
[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> 
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== 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<ref>PMID:25363287</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 2mop" style="background-color:#fffaf0;"></div>

==See Also==
*[[Disintegrin|Disintegrin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bitis arietans]]
[[Category: Large Structures]]
[[Category: Calvete J]]
[[Category: Carbajo RJ]]
[[Category: Perez A]]
[[Category: Sanz L]]