1dvi
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(New page: 200px<br /><applet load="1dvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvi, resolution 2.30Å" /> '''CALPAIN DOMAIN VI WI...)
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Revision as of 11:30, 20 November 2007
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CALPAIN DOMAIN VI WITH CALCIUM BOUND
Overview
The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain, has been determined at 2.3 A resolution, both with and without bound Ca2+., The structures reveal a unique fold incorporating five EF-hand motifs per, monomer, three of which bind calcium at physiological calcium, concentrations, with one showing a novel EF-hand coordination pattern., This investigation gives us a first view of the calcium-induced, conformational changes, and consequently an insight into the mechanism of, calcium induced activation in calpain. The crystal structures reveal a dVI, homodimer which provides a preliminary model for the subunit dimerization, in calpain.
About this Structure
1DVI 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
Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes., Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS, Cygler M, Nat Struct Biol. 1997 Jul;4(7):532-8. PMID:9228945
Page seeded by OCA on Tue Nov 20 13:37:16 2007
