1n4y: Difference between revisions
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<StructureSection load='1n4y' size='340' side='right' caption='[[1n4y]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | <StructureSection load='1n4y' size='340' side='right' caption='[[1n4y]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n4y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1n4y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Agkistrodon_rhodostoma Agkistrodon rhodostoma]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kst 1kst]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N4Y FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kst|1kst]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kst|1kst]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHOD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8717 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHOD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8717 Agkistrodon rhodostoma])</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=1n4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n4y RCSB], [http://www.ebi.ac.uk/pdbsum/1n4y PDBsum]</span></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=1n4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4y OCA], [http://pdbe.org/1n4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n4y RCSB], [http://www.ebi.ac.uk/pdbsum/1n4y PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1n4y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Disintegrin|Disintegrin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Agkistrodon rhodostoma]] | ||
[[Category: Dennis, M S]] | [[Category: Dennis, M S]] | ||
[[Category: Krane, J]] | [[Category: Krane, J]] | ||
Revision as of 08:40, 11 September 2015
REFINED STRUCTURE OF KISTRINREFINED STRUCTURE OF KISTRIN
Structural highlights
Function[VM2RH_CALRH] Metalloproteinase rhodostoxin: snake venom metalloproteinase that impairs hemostasis in the envenomed animal (By similarity). Disintegrin rhodostomin: inhibit platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). 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 PubMedThe structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist.,Adler M, Lazarus RA, Dennis MS, Wagner G Science. 1991 Jul 26;253(5018):445-8. PMID:1862345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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