Calpain: Difference between revisions
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<StructureSection load='1zcm' size=' | <StructureSection load='1zcm' size='350' side='right' caption='Human calpain1 large subunit complex with inhibitor and Ca+2 ions (green) (PDB entry [[1zcm]])' scene='51/517369/Cv/1'> | ||
__TOC__ | |||
== Function == | == Function == | ||
'''Calpains''' (CAP) are calcium-dependent cysteine proteases. CAPs are regulated by Ca+2 concentration, phosphorylation and calpastatin. 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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== Structural highlights == | == 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. | 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> | ||
*<scene name='51/517369/Cv/7'>Inhibitor binding site</scene>. Water molecules are shown as red spheres. | |||
</ | *<scene name='51/517369/Cv/8'>Covalent bond between Cys 115 of human calpain1 large subunit with inhibitor</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> | |||
==3D structures of calpain== | ==3D structures of calpain== | ||
[[Calpain 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||