Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.
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Long AM, Zhao H, Huang X
Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.
J Med Chem. 2012 Nov 26;55(22):10307-11. doi: 10.1021/jm301336n. Epub 2012 Nov 9.
- PubMed ID
- 23106386 [ View in PubMed]
- Abstract
Casein kinase 1 epsilon (CK1epsilon) and its closest homologue CK1delta are key regulators of diverse cellular processes. We report two crystal structures of PF4800567, a potent and selective inhibitor of CK1epsilon, bound to the kinase domains of human CK1epsilon and CK1delta as well as one apo CK1epsilon crystal structure. These structures provide a molecular basis for the strong and specific inhibitor interactions with CK1epsilon and suggest clues for further development of CK1delta inhibitors.