1df0: Difference between revisions

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 <StructureSection load='1df0' size='340' side='right'caption='[[1df0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1df0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DF0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1df0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DF0 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aj5|1aj5]], [[1alv|1alv]], [[1alw|1alw]], [[1dvi|1dvi]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calpain-2 Calpain-2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.53 3.4.22.53] </span></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=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [https://pdbe.org/1df0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB], [https://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1df0 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=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [http://pdbe.org/1df0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB], [http://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1df0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAN2_RAT CAN2_RAT]] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. [[http://www.uniprot.org/uniprot/CPNS1_RAT CPNS1_RAT]] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
+[https://www.uniprot.org/uniprot/CAN2_RAT CAN2_RAT] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=1df0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The combination of thiol protease activity and calmodulin-like EF-hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of the Ca(2+)-induced switch between inactive and active forms has remained elusive in the absence of structural information. We describe here the 2.6 A crystal structure of m-calpain in the Ca(2+)-free form, which illustrates the structural basis for the inactivity of calpain in the absence of Ca(2+). It also reveals an unusual thiol protease fold, which is associated with Ca(2+)-binding domains through heterodimerization and a C(2)-like beta-sandwich domain. Strikingly, the structure shows that the catalytic triad is not assembled, indicating that Ca(2+)-binding must induce conformational changes that re-orient the protease domains to form a functional active site. The alpha-helical N-terminal anchor of the catalytic subunit does not occupy the active site but inhibits its assembly and regulates Ca(2+)-sensitivity through association with the regulatory subunit. This Ca(2+)-dependent activation mechanism is clearly distinct from those of classical proteases.
-Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.,Hosfield CM, Elce JS, Davies PL, Jia Z EMBO J. 1999 Dec 15;18(24):6880-9. PMID:10601010<ref>PMID:10601010</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1df0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Calpain 3D structures|Calpain 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
-[[Category: Calpain-2]]
 [[Category: Large Structures]]
-[[Category: Davies, P L]]
+[[Category: Rattus norvegicus]]
-[[Category: Elce, J S]]
+[[Category: Davies PL]]
-[[Category: Hosfield, C M]]
+[[Category: Elce JS]]
-[[Category: Jia, Z]]
+[[Category: Hosfield CM]]
-[[Category: C2 domain]]
+[[Category: Jia Z]]
-[[Category: Calmodulin]]
-[[Category: Calpain]]
-[[Category: Catalytic triad]]
-[[Category: Cysteine protease]]
-[[Category: Hydrolase]]
-[[Category: Papain]]
-[[Category: Protease]]
-[[Category: Zymogen]]
-[[Category: Zymogen activation]]