Calpain
From Proteopedia
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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 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. <ref>PMID:11893336</ref> |
*<scene name='51/517369/Cv/3'>1st Ca+2 binding site</scene>. | *<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> | *<scene name='51/517369/Cv/2'>2nd Ca+2 binding site</scene>.<ref>PMID:16411745</ref> | ||
Revision as of 13:31, 18 November 2015
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3D structures of calpain
Updated on 18-November-2015
References
- ↑ Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL. A Ca(2+) switch aligns the active site of calpain. Cell. 2002 Mar 8;108(5):649-60. PMID:11893336
- ↑ Li Q, Hanzlik RP, Weaver RF, Schonbrunn E. Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core. Biochemistry. 2006 Jan 24;45(3):701-8. PMID:16411745 doi:http://dx.doi.org/10.1021/bi052077b
