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3.4.22.53: calpain-2

This is an abbreviated version!
For detailed information about calpain-2, go to the full flat file.

Word Map on EC 3.4.22.53

Reaction

broad endopeptidase specificity =

Synonyms

Cal II, calcium-activated neutral protease II, calpain 2, calpain II, calpain xCL-2 (Xenopus leavis), calpain-2, calpain-2-like, calpain2, CAPN II, CAPN2, CAPN2 g.p. (Homo sapiens), CPN2, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, human calpain 2, m-calpain, milli-calpain, mitochondrial m-calpain, nCL-2, rat calpain 2

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.53 calpain-2

Crystallization

Crystallization on EC 3.4.22.53 - calpain-2

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
2.6 A crystal structure of m-calpain that has a C-terminal histidine-tag and a mutation of the active site C105S in the large subunit in the Ca2+-free form
calpastatin inhibitory domain 1 crystallized with calpain 2, calpastatin inhibitory domain 4 crystallized with calpain 2
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crystallization of recombinant C105S mutant enzyme by hanging drop method
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the refined crystal structure of the mutant enzymes K226S, K230E, K234S and E504S in absence of Ca2+ are indistinguishable from wilde-type calpain
wild-type and mutant calpains