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==High resolution Structure determination of rhodocetin== | |||
<StructureSection load='1sb2' size='340' side='right'caption='[[1sb2]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1sb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SB2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1sb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sb2 OCA], [https://pdbe.org/1sb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sb2 RCSB], [https://www.ebi.ac.uk/pdbsum/1sb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sb2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SLEA_CALRH SLEA_CALRH] Potent inhibitor of collagen-induced platelet aggregation. It acts by binding to the integrin alpha2A domain and blocks collagen binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta subunits mainly contribute to this activity.<ref>PMID:10360956</ref> <ref>PMID:11121411</ref> <ref>PMID:12871211</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/sb/1sb2_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=1sb2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rhodocetin is a unique heterodimer consisting of alpha- and beta-subunits of 133 and 129 residues, respectively. The molecule, purified from the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge, unlike all the other Ca(2+)-dependent lectin-like proteins. We report here the 1.9 A resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity. | |||
Structure of rhodocetin reveals noncovalently bound heterodimer interface.,Paaventhan P, Kong C, Joseph JS, Chung MC, Kolatkar PR Protein Sci. 2005 Jan;14(1):169-75. Epub 2004 Dec 2. PMID:15576563<ref>PMID:15576563</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1sb2" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
Rhodocetin | *[[Rhodocetin|Rhodocetin]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Calloselasma rhodostoma]] | [[Category: Calloselasma rhodostoma]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chung | [[Category: Chung MCM]] | ||
[[Category: Joseph | [[Category: Joseph JS]] | ||
[[Category: Kolatkar | [[Category: Kolatkar PR]] | ||
[[Category: Kong | [[Category: Kong CG]] | ||
[[Category: Paaventhan | [[Category: Paaventhan P]] | ||
Latest revision as of 07:52, 17 October 2024
High resolution Structure determination of rhodocetinHigh resolution Structure determination of rhodocetin
Structural highlights
FunctionSLEA_CALRH Potent inhibitor of collagen-induced platelet aggregation. It acts by binding to the integrin alpha2A domain and blocks collagen binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta subunits mainly contribute to this activity.[1] [2] [3] 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 PubMedRhodocetin is a unique heterodimer consisting of alpha- and beta-subunits of 133 and 129 residues, respectively. The molecule, purified from the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge, unlike all the other Ca(2+)-dependent lectin-like proteins. We report here the 1.9 A resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity. Structure of rhodocetin reveals noncovalently bound heterodimer interface.,Paaventhan P, Kong C, Joseph JS, Chung MC, Kolatkar PR Protein Sci. 2005 Jan;14(1):169-75. Epub 2004 Dec 2. PMID:15576563[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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