1dvi: Difference between revisions
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'''CALPAIN DOMAIN VI WITH CALCIUM BOUND''' | '''CALPAIN DOMAIN VI WITH CALCIUM BOUND''' | ||
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[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
[[Category: Grochulski, P.]] | [[Category: Grochulski, P.]] | ||
[[Category: | [[Category: Calcium-dependent protease]] | ||
[[Category: | [[Category: Small subunit]] | ||
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Revision as of 11:19, 2 May 2008
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. 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 Fri May 2 14:19:48 2008
