1df0: Difference between revisions

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-[[Image:1df0.gif|left|200px]]
-<!--
+==Crystal structure of M-Calpain==
-The line below this paragraph, containing "STRUCTURE_1df0", creates the "Structure Box" on the page.
+<StructureSection load='1df0' size='340' side='right'caption='[[1df0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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='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>
-{{STRUCTURE_1df0|  PDB=1df0  |  SCENE=  }}
+</table>
+== Function ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/1df0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1df0 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF M-CALPAIN'''
+==See Also==
+*[[Calpain 3D structures|Calpain 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-DF0 is a [[Protein complex]] structure of sequences from [http://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].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/10601010 10601010]
-[[Category: Hydrolase]]
-[[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Davies, P L.]]
+[[Category: Davies PL]]
-[[Category: Elce, J S.]]
+[[Category: Elce JS]]
-[[Category: Hosfield, C M.]]
+[[Category: Hosfield CM]]
-[[Category: Jia, Z.]]
+[[Category: Jia Z]]
-[[Category: C2 domain]]
-[[Category: Calcium]]
-[[Category: Calmodulin]]
-[[Category: Calpain]]
-[[Category: Catalytic triad]]
-[[Category: Cysteine protease]]
-[[Category: Papain]]
-[[Category: Protease]]
-[[Category: Zymogen]]
-[[Category: Zymogen activation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:46:38 2008''