1mdw
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(New page: 200px<br /><applet load="1mdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdw, resolution 1.95Å" /> '''Crystal Structure of...)
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Revision as of 19:14, 20 November 2007
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Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation
Overview
Uncontrolled activation of calpain can lead to necrotic cell death and, irreversible tissue damage. We have discovered an intrinsic mechanism, whereby the autolysis-generated protease core fragment of calpain is, inactivated through the inherent instability of a key alpha-helix. This, auto-inactivation state was captured by the 1.9 A Ca(2+)-bound structure, of the protease core from m-calpain, and sequence alignments suggest that, it applies to about half of the calpain isoforms. Intact calpain large, subunits are also subject to this inhibition, which can be prevented, through assembly of the heterodimers. Other isoforms or their released, cores are not silenced by this mechanism and might contribute to calpain, patho-physiologies.
About this Structure
1MDW is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Active as Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 Full crystallographic information is available from OCA.
Reference
Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:12665854
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