Protein kinase C

spinqualitylabelsall models Rat protein kinaseα C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), 3gpe Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Protein kinase C (PKC) phosphorylates serine or threonine residues in proteins. PKC act in signal transduction pathways. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds diacylglycerol (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. Conventional PKC (CPKC) - α, β1, β2, γ – are activated by DAG, Ca+2 and a phospholipid. Novel PKC (NPKC) – δ, ε, η, θ – are activated by DAG. Atypical PKC (APKC) do not require DAG or Ca+2 for activation. Relevance Activation of PKC and elevated levels of DAG are associated with vascular abnormalities in retinal, renal and cardiovascular tissues. Inhibitors of PKC-β are tested for prevention of diabetic complications. Activation of PKC-α and PKC-β are linked to malignant phenotypes while PKC-δ is thought to mediate anti-cancer effects. Structural highlights Phosphatidylinositol binds to PKC-α C2 domain groove near the Ca+2 binding pocket. Water molecules are shown as red spheres. 3D structures of protein kinase C Protein kinase C 3D structures

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Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman