Calpain: Difference between revisions

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*<scene name='51/517369/Cv/4'>1st Ca+2 coordination site</scene>.  
*<scene name='51/517369/Cv/4'>1st Ca+2 coordination site</scene>.  
*<scene name='51/517369/Cv/5'>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>
==3D structures of calpain==
[[Calpain 3D structures]]
</StructureSection>
</StructureSection>


Revision as of 12:56, 21 April 2019

Function

Calpains (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin.[1] The CAP family contains 14 members.

  • CAP1 (or mu-CAP) and CAP2 (or M-CAP) T are the best characterized CAPs.
  • CAP7 is atypical CAP that lacks a penta-EF-hand domain.
  • CAP8 and CAP9 are involved in the mucosal defense against stress-induced gastropathies.
  • CAP9 has been identified as the tumor suppressor for gastric cancer.
  • CAP13 is expressed in testis and lungs.

Disease

CAP3 defects lead to a certain muscular dystrophy. Defective CAPs have a role in neurodegeneration.

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. [2]

  • . Water molecules are shown as red spheres.
  • .
  • .
  • .[3]

3D structures of calpain

Calpain 3D structures


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 calpain3D structures of calpain

Updated on 21-April-2019

ReferencesReferences

  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?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky
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