1df0: Difference between revisions

Revision as of 22:55, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1df0.png

Template:STRUCTURE 1df0

CRYSTAL STRUCTURE OF M-CALPAINCRYSTAL STRUCTURE OF M-CALPAIN

Template:ABSTRACT PUBMED 10601010

About this StructureAbout this Structure

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

ReferenceReference

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

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OCA

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-'''CRYSTAL STRUCTURE OF M-CALPAIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10601010}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10601010 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10601010}}
 ==About this Structure==
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 [[Category: Zymogen]]
 [[Category: Zymogen activation]]
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