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Calpain
From Proteopedia
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<StructureSection load='1zcm' size='400' side='right' caption='Human calpain1 large subunit complex with inhibitor and Ca+2 ions (green) (PDB entry [[1zcm]])' scene=''> | <StructureSection load='1zcm' size='400' side='right' caption='Human calpain1 large subunit complex with inhibitor and Ca+2 ions (green) (PDB entry [[1zcm]])' scene=''> | ||
| - | '''Calpains''' (CAP) are calcium-dependent cysteine proteases. The CAP family contains 14 members. | + | == Function == |
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| + | '''Calpains''' (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin. The CAP family contains 14 members.<br /> | ||
| + | * '''CAP1''' (or mu-CAP) and '''CAP2''' (or M-CAP) T are the best characterized CAPs. <br /> | ||
| + | * '''CAP7''' is atypical CAP that lacks a penta-EF-hand domain.<br /> | ||
| + | * '''CAP8''' and '''CAP9''' are involved in the mucosal defense against stress-induced gastropathies.<br /> | ||
| + | * '''CAP9''' has been identified as the tumor suppressor for gastric cancer.<br /> | ||
| + | * '''CAP13''' is expressed in testis and lungs. | ||
| + | |||
| + | == Structural highlights == | ||
| + | |||
| + | CAP is a heterodimer containing a small 28kDa regulatory subunit which is identical for all CAPs and a large 80kDa catalytic subunit. | ||
| + | |||
</StructureSection> | </StructureSection> | ||
Revision as of 11:34, 16 November 2015
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3D structures of calpain
Updated on 16-November-2015
