1kfu

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[[Image:1kfu.gif|left|200px]]
[[Image:1kfu.gif|left|200px]]
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{{Structure
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|PDB= 1kfu |SIZE=350|CAPTION= <scene name='initialview01'>1kfu</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1kfu", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1kfu| PDB=1kfu | SCENE= }}
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|RELATEDENTRY=[[1kfx|1KFX]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfu OCA], [http://www.ebi.ac.uk/pdbsum/1kfu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kfu RCSB]</span>
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'''Crystal Structure of Human m-Calpain Form II'''
'''Crystal Structure of Human m-Calpain Form II'''
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==About this Structure==
==About this Structure==
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1KFU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1DKV. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFU OCA].
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1KFU is a [[Protein complex]] structure of sequences from [http://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].
==Reference==
==Reference==
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[[Category: Strobl, S.]]
[[Category: Strobl, S.]]
[[Category: Suzuki, K.]]
[[Category: Suzuki, K.]]
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[[Category: calcium]]
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[[Category: Calcium]]
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[[Category: papain-like]]
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[[Category: Papain-like]]
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[[Category: regulation]]
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[[Category: Regulation]]
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[[Category: thiol-protease]]
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[[Category: Thiol-protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:41:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:01 2008''
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Revision as of 19:41, 2 May 2008

Template:STRUCTURE 1kfu

Crystal Structure of Human m-Calpain Form II


Overview

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.

About this Structure

1KFU is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1dkv. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 22:41:45 2008

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