1kxr
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(New page: 200px<br /><applet load="1kxr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kxr, resolution 2.07Å" /> '''Crystal Structure of...)
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Revision as of 17:55, 20 November 2007
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Crystal Structure of Calcium-Bound Protease Core of Calpain I
Overview
Ca(2+) signaling by calpains leads to controlled proteolysis during, processes ranging from cytoskeleton remodeling in mammals to sex, determination in nematodes. Deregulated Ca(2+) levels result in aberrant, proteolysis by calpains, which contributes to tissue damage in heart and, brain ischemias as well as neurodegeneration in Alzheimer's disease. Here, we show that activation of the protease core of mu calpain requires, cooperative binding of two Ca(2+) atoms at two non-EF-hand sites revealed, in the 2.1 A crystal structure. Conservation of the Ca(2+) binding, residues defines an ancestral general mechanism of activation for most, calpain isoforms, including some that lack EF-hand domains. The protease, region is not affected by the endogenous inhibitor, calpastatin, and may, contribute to calpain-mediated pathologies when the core is released by, autoproteolysis.
About this Structure
1KXR 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
A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:11893336
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