1sb2: Difference between revisions

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-[[Image:1sb2.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1sb2", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_1sb2|  PDB=1sb2  |  SCENE=  }}
-'''High resolution Structure determination of rhodocetin'''
+==High resolution Structure determination of rhodocetin==
+<StructureSection load='1sb2' size='340' side='right'caption='[[1sb2]], [[Resolution|resolution]] 1.90&Aring;' 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]] 1.9&#8491;</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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-SB2 is a [[Protein complex]] structure of sequences from [http://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].
+</div>
+<div class="pdbe-citations 1sb2" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15576563 15576563]
+*[[Rhodocetin|Rhodocetin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Calloselasma rhodostoma]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Chung, M C.M.]]
+[[Category: Chung MCM]]
-[[Category: Joseph, J S.]]
+[[Category: Joseph JS]]
-[[Category: Kolatkar, P R.]]
+[[Category: Kolatkar PR]]
-[[Category: Kong, C G.]]
+[[Category: Kong CG]]
-[[Category: Paaventhan, P.]]
+[[Category: Paaventhan P]]
-[[Category: C-type lectin]]
-[[Category: Domain swapping]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:29:59 2008''