Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase.

Abstract excerpt

Calpastatin is a widely distributed endogenous inhibitor protein specifically acting on calpain (Ca(2+)-dependent proteinase) and is known to interact with the calmodulin-like domain (CaMLD) of the proteinase in a Ca(2+)-dependent fashion. The calpastatin molecule consists of four inhibitory domains (domains 1-4) with mutually homologous sequences in three regions designated as A, B, and C. Acidic amphiphilic...

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