1uos

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[[Image:1uos.png|left|200px]]
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==THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN==
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<StructureSection load='1uos' size='340' side='right' caption='[[1uos]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uos]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UOS FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1umr|1umr]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uos RCSB], [http://www.ebi.ac.uk/pdbsum/1uos PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uo/1uos_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.
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{{STRUCTURE_1uos| PDB=1uos | SCENE= }}
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Structure of the snake-venom toxin convulxin.,Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891<ref>PMID:14684891</ref>
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===THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_14684891}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1uos]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:014684891</ref><references group="xtra"/>
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[[Category: Crotalus durissus terrificus]]
[[Category: Crotalus durissus terrificus]]
[[Category: Batuwangala, T.]]
[[Category: Batuwangala, T.]]

Revision as of 21:55, 29 September 2014

THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN

1uos, resolution 2.70Å

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