1mdw

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(New page: 200px<br /><applet load="1mdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdw, resolution 1.95&Aring;" /> '''Crystal Structure of...)
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[[Image:1mdw.gif|left|200px]]<br /><applet load="1mdw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mdw, resolution 1.95&Aring;" />
 
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'''Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation'''<br />
 
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==Overview==
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==Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation==
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Uncontrolled activation of calpain can lead to necrotic cell death and, irreversible tissue damage. We have discovered an intrinsic mechanism, whereby the autolysis-generated protease core fragment of calpain is, inactivated through the inherent instability of a key alpha-helix. This, auto-inactivation state was captured by the 1.9 A Ca(2+)-bound structure, of the protease core from m-calpain, and sequence alignments suggest that, it applies to about half of the calpain isoforms. Intact calpain large, subunits are also subject to this inhibition, which can be prevented, through assembly of the heterodimers. Other isoforms or their released, cores are not silenced by this mechanism and might contribute to calpain, patho-physiologies.
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<StructureSection load='1mdw' size='340' side='right'caption='[[1mdw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mdw]] 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=1MDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MDW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdw OCA], [https://pdbe.org/1mdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mdw RCSB], [https://www.ebi.ac.uk/pdbsum/1mdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mdw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/md/1mdw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1mdw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MDW OCA].
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*[[Calpain 3D structures|Calpain 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12665854 12665854]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Davies PL]]
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[[Category: Davies, P.L.]]
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[[Category: Hosfield CM]]
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[[Category: Hosfield, C.M.]]
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[[Category: Jia Z]]
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[[Category: Jia, Z.]]
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[[Category: Lim D]]
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[[Category: Lim, D.]]
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[[Category: Moldoveanu T]]
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[[Category: Moldoveanu, T.]]
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[[Category: CA]]
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[[Category: calpain cysteine protease fold]]
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[[Category: helix instability]]
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[[Category: tryptophan-based active site blockage]]
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[[Category: two cooperative calcium sites]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:21:13 2007''
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Current revision

Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation

PDB ID 1mdw

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