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. 2011 May 3;6(5):e19035. doi: 10.1371/journal.pone.0019035

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duVerle et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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“Conventional” calpains (- and m-calpain) are composed of larger catalytic subunits (calpain-1 and -2) and a smaller regulatory subunit. Some homologues, such as skeletal muscle-specific calpain (calpain-3/p94) have slightly diverged properties, including unique insertion sequences (NS, IS1 and IS2) and no requirement for a small subunit. Symbols used are: I: N-terminal domain with little homology; IIa and IIb: protease sub-domains containing the active sites Cys and His/Asn, respectively; III: C2-like -binding domain; IV and VI: 5-EF-hand -binding domain; V: Gly-rich hydrophobic domain; NS, IS1 and IS2: p94-specific sequences.

Inline graphic — “Conventional” calpains (- and m-calpain) are composed of larger catalytic subunits (calpain-1 and -2) and a smaller regulatory subunit. Some homologues, such as skeletal muscle-specific calpain (calpain-3/p94) have slightly diverged properties, including unique insertion sequences (NS, IS1 and IS2) and no requirement for a small subunit. Symbols used are: I: N-terminal domain with little homology; IIa and IIb: protease sub-domains containing the active sites Cys and His/Asn, respectively; III: C2-like -binding domain; IV and VI: 5-EF-hand -binding domain; V: Gly-rich hydrophobic domain; NS, IS1 and IS2: p94-specific sequences.