View source for 1drs


==THREE-DIMENSIONAL STRUCTURE OF THE RGD-CONTAINING NEUROTOXIN HOMOLOGUE, DENDROASPIN==
<StructureSection load='1drs' size='340' side='right'caption='[[1drs]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1drs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_jamesoni_kaimosae Dendroaspis jamesoni kaimosae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 39 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=1drs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drs OCA], [https://pdbe.org/1drs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1drs RCSB], [https://www.ebi.ac.uk/pdbsum/1drs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1drs ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/3SPM_DENJA 3SPM_DENJA] Inhibits ADP-induced platelet aggregation and inhibits the binding of purified platelet fibrinogen receptor alpha-IIb/beta-3 (ITGA2B/ITGB3) to immobilized fibrinogen (PubMed:1591238). Has also been described to inhibit cell adhesion to fibrinogen, fibronectin, laminin and collagen (PubMed:11336631, PubMed:16798616).<ref>PMID:11336631</ref> <ref>PMID:1591238</ref> <ref>PMID:16798616</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dr/1drs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1drs ConSurf].
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== Publication Abstract from PubMed ==
Dendroaspin is a short chain neurotoxin homologue from the venom of Elapidae snakes, which lacks neurotoxicity. Unlike neurotoxins, it contains an Arg-Gly-Asp-(RGD)-motif and functions as an inhibitor of platelet aggregation and platelet adhesion with comparable potency to the disintegrins from the venoms of Viperidae. We have determined the structure of dendroaspin in solution using NMR spectroscopy. The structure contains a core similar to that of short chain neurotoxins, but with a novel arrangement of loops and a solvent-exposed RGD-motif. Dendroaspin is thus an integrin antagonist with a well defined fold different from that of the disintegrins, based on the neurotoxin scaffold.

Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin.,Sutcliffe MJ, Jaseja M, Hyde EI, Lu X, Williams JA Nat Struct Biol. 1994 Nov;1(11):802-7. PMID:7634091<ref>PMID:7634091</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dendroaspis jamesoni kaimosae]]
[[Category: Large Structures]]
[[Category: Hyde EI]]
[[Category: Jaseja M]]
[[Category: Lu X]]
[[Category: Sutcliffe MJ]]
[[Category: Williams JA]]