Protein kinase C: Difference between revisions
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Michal Harel (talk | contribs) No edit summary |
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{{STRUCTURE_3pge| PDB=3pge | SIZE=400| SCENE= |right|CAPTION=Rat protein kinase a C2 domain complex with phosphatidylinositol and Ca+2 ion, [[3pge]] }} | |||
'''Protein kinase C''' (PKC) phosphorylate serine or threonine residues in proteins. They act in signal transduction pathways. Conventional PKC (CPKC) - a, b1, b2, g – are activated by diacylglycerol (DAG), Ca+2 and a phospholipid. Novel PKC (NPKC) – d, e, eta, theta – are activated by DAG. Atypical (APKC) do not require DAG or Ca+2 for activation. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds DAG and phorbol esters and the C2 domain which is a Ca+2 sensor. PKC contains Pleckstrin Homology (PH) domain which binds phosphatidylinositol lipids (PTDINS). The PH domain is found in proteins involved in intracellular signaling. | '''Protein kinase C''' (PKC) phosphorylate serine or threonine residues in proteins. They act in signal transduction pathways. Conventional PKC (CPKC) - a, b1, b2, g – are activated by diacylglycerol (DAG), Ca+2 and a phospholipid. Novel PKC (NPKC) – d, e, eta, theta – are activated by DAG. Atypical (APKC) do not require DAG or Ca+2 for activation. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds DAG and phorbol esters and the C2 domain which is a Ca+2 sensor. PKC contains Pleckstrin Homology (PH) domain which binds phosphatidylinositol lipids (PTDINS). The PH domain is found in proteins involved in intracellular signaling. | ||
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==3D structures of protein kinase C== | ==3D structures of protein kinase C== | ||
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[[2d9z]] – hPKC-nu PH domain - NMR | [[2d9z]] – hPKC-nu PH domain - NMR | ||
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