Calpain

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'''Calpains''' (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin.<ref>PMID:12843408</ref> The CAP family contains 14 members.<br />
'''Calpains''' (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin.<ref>PMID:12843408</ref> The CAP family contains 14 members.<br />
* '''CAP1''' (or mu-CAP) and '''CAP2''' (or M-CAP) T are the best characterized CAPs. <br />
* '''CAP1''' (or mu-CAP) and '''CAP2''' (or M-CAP) T are the best characterized CAPs. <br />
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* '''CAP2''' limits the extent of neuronal plasticity and learning<ref>PMID:33339205</ref>.
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* '''CAP3''' is expressed in skeletal muscles and regulates sarcomere remodelling<ref>PMID:16884488</ref>.
* '''CAP7''' is atypical CAP that lacks a penta-EF-hand domain.<br />
* '''CAP7''' is atypical CAP that lacks a penta-EF-hand domain.<br />
* '''CAP8''' and '''CAP9''' are involved in the mucosal defense against stress-induced gastropathies.<br />
* '''CAP8''' and '''CAP9''' are involved in the mucosal defense against stress-induced gastropathies.<br />
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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>
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</StructureSection>
 
==3D structures of calpain==
==3D structures of calpain==
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[[Calpain 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*CAP small subunit
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**[[1aj5]]– rCAP domain VI – rat<br />
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**[[1dvi]] - rCAP domain VI + Ca<br />
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**[[1np8]] – rCAP residues 87-245 - Cd<br />
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**[[1alv]], [[1nx2]] - pCAP domain VI + Ca – pig<br />
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**[[1alw]], [[1nx3]] - pCAP domain VI + Ca+ inhibitor<br />
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**[[1nx0]] - pCAP domain VI + Ca+ Calpastatin peptide + small molecule inhibitor peptide<br />
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**[[1nx1]] - pCAP domain VI + Ca+ Calpastatin peptide<br />
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**[[4phj]] – hCAP EF-hand subunit + Ca - human<br />
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**[[4phk]], [[4phm]], [[4phn]], [[4wq2]], [[4wq3]], [[5d69]] – hCAP EF-hand subunit + Ca + inhibitor<br />
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*CAP1
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**[[1kxr]], [[1tlo]], [[1qxp]] - rCAP protease domain + Ca<br />
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**[[1tl9]] - rCAP protease domain + Ca+ leupeptin inhibitor<br />
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**[[2g8e]], [[2g8j]], [[2nqg]], [[2nqi]], [[2r9c]], [[2r9f]] - rCAP protease domain + Ca+ inhibitor<br />
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**[[2ary]] - hCAP protease domain + Ca <br />
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**[[1zcm]] - hCAP protease domain (mutant) + Ca+ inhibitor<br />
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*CAP2
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**[[1mdw]] – rCAP2 protease core domain I and II (mutant) + Ca<br />
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**[[1df0]], [[1u5i]] – rCAP small subunit domain VI + rCAP2 large subunit<br />
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**[[3df0]] - hCAP small subunit + hCAP2 large subunit + Calpastatin + Ca<br />
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**[[3bow]] - rCAP small subunit + rCAP2 large subunit + Calpastatin + Ca<br />
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**[[1kfu]], [[1kfx]] – hCAP small subunit + hCAP2 large subunit
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*CAP3
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**[[4okh]] - hCAP EF-hand domain residues 642-821<br />
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**[[6bdt]], [[6bgp]] - hCAP residues 46-419 (mutant)<br />
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**[[6bjd]] - hCAP residues 46-419 + sorbitol + guanidine derivative<br />
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**[[6bkj]] - hCAP residues 46-419 + leupeptin peptide<br />
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*CAP7
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**[[2qfe]] - hCAP C2-like domain
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*CAP8
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**[[2nqa]] - hCAP protease domain + Ca+ leupeptin inhibitor<br />
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*CAP9
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**[[1ziv]] – hCAP catalytic domain<br />
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**[[2p0r]] - hCAP protease domain + Ca+ leupeptin inhibitor<br />
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*CAP13
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**[[2i7a]] – hCAP domain IV + Ca<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

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. ↑ Wang Y, Liu Y, Bi X, Baudry M. Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death. Cells. 2020 Dec 16;9(12):2698. PMID:33339205 doi:10.3390/cells9122698
  3. ↑ Duguez S, Bartoli M, Richard I. Calpain 3: a key regulator of the sarcomere? FEBS J. 2006 Aug;273(15):3427-36. PMID:16884488 doi:10.1111/j.1742-4658.2006.05351.x
  4. ↑ 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
  5. ↑ 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

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