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<StructureSection load='1kfu' size='340' side='right'caption='[[1kfu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1kfu' size='340' side='right'caption='[[1kfu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kfu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dkv 1dkv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1kfu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dkv 1dkv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFU FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kfx|1kfx]]</div></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]] 2.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calpain-2 Calpain-2], with EC number [https://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=1kfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfu OCA], [https://pdbe.org/1kfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfu RCSB], [https://www.ebi.ac.uk/pdbsum/1kfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfu ProSAT]</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=1kfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfu OCA], [https://pdbe.org/1kfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfu RCSB], [https://www.ebi.ac.uk/pdbsum/1kfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CAN2_HUMAN CAN2_HUMAN]] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. [[https://www.uniprot.org/uniprot/CPNS1_HUMAN CPNS1_HUMAN]] 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_HUMAN CAN2_HUMAN] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1kfu ConSurf].
</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=1kfu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in processes such as cytoskeleton remodeling and signal transduction. The 2.3-A crystal structure of full-length heterodimeric [80-kDa (dI-dIV) + 30-kDa (dV+dVI)] human m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin-like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich domain dIII and the N-terminal segments dI+dV located between. Compared with papain, the two subdomains dIIa+dIIb of the catalytic unit are rotated against one another by 50 degrees, disrupting the active site and the substrate binding site, explaining the inactivity of calpains in the absence of calcium. Calcium binding to an extremely negatively charged loop of domain dIII (an electrostatic switch) could release the adjacent barrel-like subdomain dIIb to move toward the helical subdomain dIIa, allowing formation of a functional catalytic center. This switch loop could also mediate membrane binding, thereby explaining calpains' strongly reduced calcium requirements in vivo. The activity status at the catalytic center might be further modulated by calcium binding to the calmodulin domains via the N-terminal linkers.
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.,Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):588-92. PMID:10639123<ref>PMID:10639123</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kfu" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Calpain 3D structures|Calpain 3D structures]]
*[[Calpain 3D structures|Calpain 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Calpain-2]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bartunik, H]]
[[Category: Bartunik H]]
[[Category: Bode, W]]
[[Category: Bode W]]
[[Category: Bourenkow, G]]
[[Category: Bourenkow G]]
[[Category: Braun, M]]
[[Category: Braun M]]
[[Category: Fernandez-Catalan, C]]
[[Category: Fernandez-Catalan C]]
[[Category: Huber, R]]
[[Category: Huber R]]
[[Category: Irie, A]]
[[Category: Irie A]]
[[Category: Masumoto, H]]
[[Category: Masumoto H]]
[[Category: Nakagawa, K]]
[[Category: Nakagawa K]]
[[Category: Sorimachi, H]]
[[Category: Sorimachi H]]
[[Category: Strobl, S]]
[[Category: Strobl S]]
[[Category: Suzuki, K]]
[[Category: Suzuki K]]
[[Category: Hydrolase]]
[[Category: Papain-like]]
[[Category: Regulation]]
[[Category: Thiol-protease]]

Latest revision as of 07:46, 7 February 2024

Crystal Structure of Human m-Calpain Form II

1kfu, resolution 2.50Å

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