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

  • Zongchao Jia
  • Christopher M. Hosfield
  • Peter L. Davies
  • John S. Elce
Part of the Methods in Molecular Biology™ book series (MIMB, volume 172)

Abstract

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).

Keywords

Cysteine Protease Catalytic Subunit Regulatory Subunit Catalytic Triad Thiol Protease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 2002

Authors and Affiliations

  • Zongchao Jia
    • 1
  • Christopher M. Hosfield
    • 1
  • Peter L. Davies
    • 1
  • John S. Elce
    • 1
  1. 1.Department of BiochemistryQueen’s University and the Protein Engineering Network of Centres of ExcellenceKingstonCanada

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