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Calpain

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

Revision as of 11:51, 9 January 2019

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

Drag the structure with the mouse to rotate

3D structures of calpain

Updated on 09-January-2019

References

  1. ↑ Goll DE, Thompson VF, Li H, Wei W, Cong J. The calpain system. Physiol Rev. 2003 Jul;83(3):731-801. PMID:12843408 doi:http://dx.doi.org/10.1152/physrev.00029.2002
  2. ↑ 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
  3. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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