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==REFINED STRUCTURE OF KISTRIN==
==REFINED STRUCTURE OF KISTRIN==
<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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1n4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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 Agkistrodon rhodostoma])</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=1n4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4y OCA], [https://pdbe.org/1n4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4y RCSB], [https://www.ebi.ac.uk/pdbsum/1n4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4y ProSAT]</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 ==
[[http://www.uniprot.org/uniprot/VM2RH_CALRH 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).  
[https://www.uniprot.org/uniprot/VM2RH_CALRH 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/1n4y_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/1n4y_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 19: Line 19:
</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=1n4y ConSurf].
</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=1n4y ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:1862345</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n4y" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Disintegrin|Disintegrin]]
*[[Disintegrin|Disintegrin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agkistrodon rhodostoma]]
[[Category: Calloselasma rhodostoma]]
[[Category: Dennis, M S]]
[[Category: Large Structures]]
[[Category: Krane, J]]
[[Category: Dennis MS]]
[[Category: Krezel, A M]]
[[Category: Krane J]]
[[Category: Lazarus, R A]]
[[Category: Krezel AM]]
[[Category: Wagner, G]]
[[Category: Lazarus RA]]
[[Category: Beta]]
[[Category: Wagner G]]
[[Category: Blood clotting]]
[[Category: Blood coagulation]]
[[Category: Rgd]]
[[Category: Venom]]

Latest revision as of 11:45, 10 April 2024

REFINED STRUCTURE OF KISTRINREFINED STRUCTURE OF KISTRIN

Structural highlights

1n4y is a 1 chain structure with sequence from Calloselasma rhodostoma. This structure supersedes the now removed PDB entry 1kst. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

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