Abstract
The crystal structure of a Ca2+-binding domain (dVI) of rat m-calpain has been determined at 2.3 Å 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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Blanchard, H., Grochulski, P., Li, Y. et al. Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes. Nat Struct Mol Biol 4, 532–538 (1997). https://doi.org/10.1038/nsb0797-532
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DOI: https://doi.org/10.1038/nsb0797-532
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