Phosphatidylinositol 4-kinase

spinqualitylabelsall models Human phosphatidylinositol 4-kinase IIIβ complex with an inhibitor (PDB code 4wag) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Phosphatidylinositol 4-kinase (PI4K) modulates inter-organelle lipid tarfficking. phosphoinositide signalling and intracellular vescicle trafficking. The catalytic domain of PI4K is required for the synthesis of phosphatidylinositol 4-phosphate. The mammalian PI4K are classified into 2 types - II and III - based on their molecular mass and modulation by detergent and adenosine. Phosphatidylinositol 4-kinase IIα accounts for the bulk of PI4K activity in the brain and is concentrated at synapses. Phosphatidylinositol 4-kinase IIβ synthesises phosphatidylinositok 4,5-bisphosphate at the plasma membrane. Phosphatidylinositol 4-kinase IIIα catalyses the synthesis of phosphatidylinositol 4-phosphate in hepatitis C virus cells. Phosphatidylinositol 4-kinase IIIβ is a key enzyme in the control of spingomyelin synthesis by controlling the flow of ceramide from the endoplasmic reticulum to the Golgi compartment. Relevance Phosphatidylinositol 4-kinase IIIβ is required for cellular entry by pseudoviruses bearing the SARS-CoV spike protein. Inhibitors of hPI4KIIIβ blocked the entry of SARS pseudoviruses into cells. Structural highlights The 3D structure of phosphatidylinositol 4-kinase IIIβ complex with an inhibitor shows the inhibitor lying in the ATP binding pocket making various hydrophobic interactions and hydrogen bonds to the enzyme. Based on superposition of this structure on others with PI4K bound to ATP it is evident that the inhibitor's 5-member ring overlap the adenine ring of ATP suggesting that this inhibitor functions by sterically blocking the binding of ATP to the enzyme.

3D structures of phosphatidylinositol 4-kinase

Phosphatidylinositol 4-kinase 3D structures

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Michal Harel, Alexander Berchansky