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The calcium-binding domains of calpain are crucial for regulating its activity as an intracellular cysteine protease. These domains, including the CysPc, CBSW/C2-like, and PEF-hand regions, bind calcium ions, triggering conformational changes that activate the enzyme. This activation allows calpain to perform limited proteolysis of target proteins, modulating their function and contributing to processes like cytoskeletal remodeling, cell signaling, and apoptosis. Calpain's activity is also regulated by its endogenous inhibitor, calpastatin, whose interaction is calcium-dependent.
N/A. This is a domain, not a drug.
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