1dvi
From Proteopedia
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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 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
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