Calpain
From Proteopedia
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CAP is a heterodimer containing a small 28kDa regulatory subunit which is identical for all CAPs and a large 80kDa catalytic subunit. CAP undergoes conformational change upon binding of Ca+2 ions resulting in closing of its active site cleft and activation as a cysteine protease. | CAP is a heterodimer containing a small 28kDa regulatory subunit which is identical for all CAPs and a large 80kDa catalytic subunit. CAP undergoes conformational change upon binding of Ca+2 ions resulting in closing of its active site cleft and activation as a cysteine protease. | ||
| - | + | *<scene name='51/517369/Cv/3'>1st Ca+2 binding site</scene>. | |
| + | *<scene name='51/517369/Cv/2'>2nd Ca+2 binding site</scene>.<ref>PMID:16411745</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:28, 18 November 2015
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3D structures of calpain
Updated on 18-November-2015
