Calpain
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Revision as of 14:43, 13 January 2016 by Alexander Berchansky (talk | contribs)
ContentsFunctionCalpains (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin.[1] The CAP family contains 14 members.
DiseaseCAP3 defects lead to a certain muscular dystrophy. Defective CAPs have a role in neurodegeneration. Structural highlightsCAP 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]
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3D structures of calpain
Updated on 13-January-2016
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- CAP small subunit
- 1aj5– rCAP domain VI – rat
- 1dvi - rCAP domain VI + Ca
- 1np8 – rCAP residues 87-245 - Cd
- 1alv, 1nx2 - pCAP domain VI + Ca – pig
- 1alw, 1nx3 - pCAP domain VI + Ca+ inhibitor
- 1nx0 - pCAP domain VI + Ca+ Calpastatin peptide + small molecule inhibitor peptide
- 1nx1 - pCAP domain VI + Ca+ Calpastatin peptide
- 4phj – hCAP EF-hand subunit + Ca - human
- 4phk, 4phm, 4phn – hCAP EF-hand subunit + Ca + inhibitor
- 1aj5– rCAP domain VI – rat
- CAP1
- CAP2
- 1mdw – rCAP2 protease core domain I and II (mutant) + Ca
- 1df0, 1u5i – rCAP small subunit domain VI + rCAP2 large subunit
- 3df0 - hCAP small subunit + hCAP2 large subunit + Calpastatin + Ca
- 3bow - rCAP small subunit + rCAP2 large subunit + Calpastatin + Ca
- 1kfu, 1kfx – hCAP small subunit + hCAP2 large subunit
- 1mdw – rCAP2 protease core domain I and II (mutant) + Ca
- CAP3
- 4okh - hCAP EF-hand domain
- 4okh - hCAP EF-hand domain
- CAP7
- 2qfe - hCAP C2-like domain
- CAP8
- 2nqa - hCAP protease domain + Ca+ leupeptin inhibitor
- 2nqa - hCAP protease domain + Ca+ leupeptin inhibitor
- CAP9
- CAP13
- 2i7a – hCAP domain IV + Ca
- 2i7a – hCAP domain IV + Ca
References
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