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Title
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Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes.
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Authors
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H.Blanchard,
P.Grochulski,
Y.Li,
J.S.Arthur,
P.L.Davies,
J.S.Elce,
M.Cygler.
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Ref.
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Nat Struct Biol, 1997,
4,
532-538.
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PubMed id
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Abstract
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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.
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