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Literature summary for 3.4.22.53 extracted from

  • Strobl S.; Fernandez-Catalan C.; Braun M.; Huber R.; Masumoto H.; Nakagawa K.; Irie A.; Sorimachi H.; Bourenkow G.; Bartunik H.; Suzuki K.; Bode W.
    The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium (2000), Proc. Natl. Acad. Sci. USA, 97, 588-592.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
full-length human m-calpain containing an N-terminal Gly-Arg-Arg-Asp-Arg-Ser L-chain elongation overexpressed in a baculovirus expression system. Crystals grown by vapor diffusion. The 2.3 A crystal structure of full length heterodimeric m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin, like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich domain dIII and the N-terminal segments dI+dV located between Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens enzyme is involved in cytoskeleton remodelling and signal transduction ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens P17655
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is involved in cytoskeleton remodelling and signal transduction Homo sapiens ?
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