Calpain: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


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.
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.


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Revision as of 12:02, 16 November 2015

Human calpain1 large subunit complex with inhibitor and Ca+2 ions (green) (PDB entry 1zcm)

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3D structures of calpain

Updated on 16-November-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky