Calpain
From Proteopedia
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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 /> | ||
| + | * '''CAP2''' limits the extent of neuronal plasticity and learning<ref>PMID:33339205</ref>. | ||
| + | * '''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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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of calpain== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *CAP small subunit | ||
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| - | **[[1aj5]]– rCAP domain VI – rat<br /> | ||
| - | **[[1dvi]] - rCAP domain VI + Ca<br /> | ||
| - | **[[1np8]] – rCAP residues 87-245 - Cd<br /> | ||
| - | **[[1alv]], [[1nx2]] - pCAP domain VI + Ca – pig<br /> | ||
| - | **[[1alw]], [[1nx3]] - pCAP domain VI + Ca+ inhibitor<br /> | ||
| - | **[[1nx0]] - pCAP domain VI + Ca+ Calpastatin peptide + small molecule inhibitor peptide<br /> | ||
| - | **[[1nx1]] - pCAP domain VI + Ca+ Calpastatin peptide<br /> | ||
| - | **[[4phj]] – hCAP EF-hand subunit + Ca - human<br /> | ||
| - | **[[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 /> | ||
| - | **[[1tl9]] - rCAP protease domain + Ca+ leupeptin inhibitor<br /> | ||
| - | **[[2g8e]], [[2g8j]], [[2nqg]], [[2nqi]], [[2r9c]], [[2r9f]] - rCAP protease domain + Ca+ inhibitor<br /> | ||
| - | **[[2ary]] - hCAP protease domain + Ca <br /> | ||
| - | **[[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 /> | ||
| - | **[[1df0]], [[1u5i]] – rCAP small subunit domain VI + rCAP2 large subunit<br /> | ||
| - | **[[3df0]] - hCAP small subunit + hCAP2 large subunit + Calpastatin + Ca<br /> | ||
| - | **[[3bow]] - rCAP small subunit + rCAP2 large subunit + Calpastatin + Ca<br /> | ||
| - | **[[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 /> | ||
| - | **[[6bdt]], [[6bgp]] - hCAP residues 46-419 (mutant)<br /> | ||
| - | **[[6bjd]] - hCAP residues 46-419 + sorbitol + guanidine derivative<br /> | ||
| - | **[[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 /> | ||
| - | **[[2p0r]] - hCAP protease domain + Ca+ leupeptin inhibitor<br /> | ||
| - | |||
| - | *CAP13 | ||
| - | |||
| - | **[[2i7a]] – hCAP domain IV + Ca<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
