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1df0

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[[Image:1df0.gif|left|200px]]
[[Image:1df0.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1df0 |SIZE=350|CAPTION= <scene name='initialview01'>1df0</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1df0", creates the "Structure Box" on the page.
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|SITE=
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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_1df0| PDB=1df0 | SCENE= }}
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|RELATEDENTRY=[[1aj5|1AJ5]], [[1alv|1ALV]], [[1alw|1ALW]], [[1dvi|1DVI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [http://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB]</span>
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'''CRYSTAL STRUCTURE OF M-CALPAIN'''
'''CRYSTAL STRUCTURE OF M-CALPAIN'''
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[[Category: Hosfield, C M.]]
[[Category: Hosfield, C M.]]
[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
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[[Category: c2 domain]]
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[[Category: C2 domain]]
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[[Category: calcium]]
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[[Category: Calcium]]
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[[Category: calmodulin]]
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[[Category: Calmodulin]]
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[[Category: calpain]]
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[[Category: Calpain]]
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[[Category: catalytic triad]]
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[[Category: Catalytic triad]]
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[[Category: cysteine protease]]
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[[Category: Cysteine protease]]
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[[Category: papain]]
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[[Category: Papain]]
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[[Category: protease]]
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[[Category: Protease]]
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[[Category: zymogen]]
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[[Category: Zymogen]]
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[[Category: zymogen activation]]
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[[Category: Zymogen activation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:46:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:18 2008''
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Revision as of 10:46, 2 May 2008

Image:1df0.gif

Template:STRUCTURE 1df0

CRYSTAL STRUCTURE OF M-CALPAIN


Overview

The combination of thiol protease activity and calmodulin-like EF-hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of the Ca(2+)-induced switch between inactive and active forms has remained elusive in the absence of structural information. We describe here the 2.6 A crystal structure of m-calpain in the Ca(2+)-free form, which illustrates the structural basis for the inactivity of calpain in the absence of Ca(2+). It also reveals an unusual thiol protease fold, which is associated with Ca(2+)-binding domains through heterodimerization and a C(2)-like beta-sandwich domain. Strikingly, the structure shows that the catalytic triad is not assembled, indicating that Ca(2+)-binding must induce conformational changes that re-orient the protease domains to form a functional active site. The alpha-helical N-terminal anchor of the catalytic subunit does not occupy the active site but inhibits its assembly and regulates Ca(2+)-sensitivity through association with the regulatory subunit. This Ca(2+)-dependent activation mechanism is clearly distinct from those of classical proteases.

About this Structure

1DF0 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation., Hosfield CM, Elce JS, Davies PL, Jia Z, EMBO J. 1999 Dec 15;18(24):6880-9. PMID:10601010 Page seeded by OCA on Fri May 2 13:46:38 2008

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