1qxp

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[[Image:1qxp.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of a mu-like calpain==
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|PDB= 1qxp |SIZE=350|CAPTION= <scene name='initialview01'>1qxp</scene>, resolution 2.80&Aring;
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<StructureSection load='1qxp' size='340' side='right'caption='[[1qxp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1qxp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QXP FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Calpain-1 Calpain-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 3.4.22.52] </span>
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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]] 2.8&#8491;</td></tr>
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|GENE=
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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=1qxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxp OCA], [https://pdbe.org/1qxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qxp RCSB], [https://www.ebi.ac.uk/pdbsum/1qxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxp ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1df0|1DF0]], [[1dkv|1DKV]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxp OCA], [http://www.ebi.ac.uk/pdbsum/1qxp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qxp RCSB]</span>
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[https://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/CAN1_RAT CAN1_RAT] Calcium-regulated non-lysosomal thiol-protease which catalyze 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.
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}}
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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/qx/1qxp_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=1qxp ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of a mu-like calpain'''
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==See Also==
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*[[Calpain 3D structures|Calpain 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The two Ca2+-dependent cysteine proteases, micro- and m-calpain, are involved in various Ca2+-linked signal pathways but differ markedly in their Ca2+ requirements for activation. We have determined the structure of a micro-like calpain, which has 85% micro-calpain sequence (the first 48 and the last 62 residues of the large subunit are those from m-calpain) and a low Ca2+ requirement. This construct was used because micro-calpain itself is too poorly expressed. The structure of micro-like calpain is very similar in overall fold to that of m-calpain as expected, but differs significantly in two aspects. In comparison with m-calpain, the catalytic triad residues in micro-like calpain, His and Cys, are much closer together in the absence of Ca2+, and significant portions of the Ca2+ binding EF-hand motifs are disordered and more flexible. These structural differences imply that Ca2+-free micro-calpain may represent a partially activated structure, requiring lower Ca2+ concentration to trigger its activation.
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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==About this Structure==
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1QXP is a [[Single protein]] structure of sequence 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=1QXP OCA].
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==Reference==
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Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement., Pal GP, De Veyra T, Elce JS, Jia Z, Structure. 2003 Dec;11(12):1521-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14656436 14656436]
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[[Category: Calpain-1]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Elce JS]]
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[[Category: Elce, J S.]]
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[[Category: Jia Z]]
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[[Category: Jia, Z.]]
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[[Category: Pal GP]]
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[[Category: Pal, G P.]]
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[[Category: Veyra TD]]
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[[Category: Veyra, T D.]]
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[[Category: ca(2+) requirement]]
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[[Category: catalytic triad]]
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[[Category: m-calpain]]
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[[Category: mu-calpain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:30 2008''
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Current revision

Crystal Structure of a mu-like calpain

PDB ID 1qxp

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