SpringerProtocols: Abstract: Crystal Structure of Calpain and Insights into Ca2+-Dependent Activation

Crystal Structure of Calpain and Insights into Ca2+-Dependent Activation

By: Zongchao Jia², Christopher M. Hosfield², Peter L. Davies², John S. Elce²

Abstract

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Calpains are the only known enzymes that combine protease activity with a dependence on Ca²⁺-binding to EF-hands in one molecule. The μ- and m-calpains are cytosolic cysteine proteases that are ubiquitously expressed and differ in their sensitivity to Ca²⁺. They consist of an isoform-specific catalytic approx 80-kDa subunit and a common regulatory approx 28-kDa subunit. Although the exact physiological roles of calpains remain to be elucidated, their functional characteristics and wide distribution suggest that they have important cellular roles, which have been reviewed elsewhere (1-4).

Affiliation(s): (2) Department of Biochemistry, Queen’s University and the Protein Engineering Network of Centres of Excellence, Kingston, ON, Canada

Book Title: Calcium-Binding Protein Protocols: Volume 1: Reviews and Case Studies

Series: Methods in Molecular Biology | Volume: 172 | Pub. Date: Jan-02-2002 | Page Range: 51-67 | DOI: 10.1385/1-59259-183-3:051

Subject: Protein Science

References

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