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Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes

Nature Structural Biology volume 4, pages 532–538 (1997)Cite this article

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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Authors and Affiliations

  1. Biotechnology Research Institute, NRC, Montréal, Québec, H4P 2R2, Canada

    Helen Blanchard, Pawel Grochulski, Yunge Li & Miroslaw Cygler

  2. Institute of Physics, Technical University of Lodz, 93-005, Lodz, Poland

    Pawel Grochulski

  3. Department of Biochemistry, Queen's University, Kingston, Ontario, K7L 3N6, Canada

    J. Simon C. Arthur, Peter L. Davies & John S. Elce

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  1. Helen Blanchard
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  2. Pawel Grochulski
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  6. John S. Elce
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  7. Miroslaw Cygler
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Correspondence to Miroslaw Cygler.

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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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