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| | ==Crystal Structure of Human m-Calpain Form I== | | ==Crystal Structure of Human m-Calpain Form I== |
| - | <StructureSection load='1kfx' size='340' side='right' caption='[[1kfx]], [[Resolution|resolution]] 3.15Å' scene=''> | + | <StructureSection load='1kfx' size='340' side='right'caption='[[1kfx]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kfx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kfx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kfu|1kfu]]</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]] 3.15Å</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=1kfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfx OCA], [https://pdbe.org/1kfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfx RCSB], [https://www.ebi.ac.uk/pdbsum/1kfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfx 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=1kfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfx OCA], [http://pdbe.org/1kfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfx RCSB], [http://www.ebi.ac.uk/pdbsum/1kfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://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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| | </div> | | </div> |
| | <div class="pdbe-citations 1kfx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1kfx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Calpain 3D structures|Calpain 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Calpain-2]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[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]]
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| - | [[Category: Thiol-protease]]
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| Structural highlights
Function
CAN2_HUMAN Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):588-92. PMID:10639123
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