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J Med Chem. 2012 Nov 26;55(22):10307-11. doi: 10.1021/jm301336n. Epub 2012 Nov 9.

Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.

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1
Department of Molecular Structure and Characterization, Amgen Inc., 360 Binney Street, Cambridge, Massachusetts 02142, USA.

Abstract

Casein kinase 1 epsilon (CK1ε) and its closest homologue CK1δ are key regulators of diverse cellular processes. We report two crystal structures of PF4800567, a potent and selective inhibitor of CK1ε, bound to the kinase domains of human CK1ε and CK1δ as well as one apo CK1ε crystal structure. These structures provide a molecular basis for the strong and specific inhibitor interactions with CK1ε and suggest clues for further development of CK1δ inhibitors.

PMID:
23106386
DOI:
10.1021/jm301336n
[Indexed for MEDLINE]
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