Dual specificity protein kinase

spinqualitylabelsall models Dual specificity protein kinase TTK kinase domain complex with inhibitor, 2x9e Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Dual specificity protein kinases are kinases which act as both tyrosine kinase and serine/threonine kinase. CLK1 phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing. Clk2 and Clk3 cause the redistribution of SR proteins and can regulate the alternative splicing of precursor mRNA. CLK4 phosphorylates tyrosine or serine/threonine. Structural highlights The dual specificity protein kinase TTK or monopolar spindle kinase 1 contains tetratricopeptide repeat domain (TPR) which serves as interaction domain between proteins. The TPR domain is a helical 34 amino acid motif which is found in several copies in a protein which fold together forming a protein-protein binding domain. Cancer therapy potential drugs bind in TTK active site. 3D structures of dual specificity protein kinase Dual specificity protein kinase 3D structures

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