Calpain: Difference between revisions

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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. <ref>PMID:11893336</ref>
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. <ref>PMID:11893336</ref>
*<scene name='51/517369/Cv/3'>1st Ca+2 coordination site</scene>.
*<scene name='51/517369/Cv/4'>1st Ca+2 coordination site</scene>. Water molecules are shown as red spheres.
*<scene name='51/517369/Cv/2'>2nd Ca+2 coordination site</scene>.<ref>PMID:16411745</ref>
*<scene name='51/517369/Cv/5'>2nd Ca+2 coordination site</scene>.<ref>PMID:16411745</ref>
</StructureSection>
</StructureSection>


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Michal Harel, Alexander Berchansky