Download MendeleyStructural basis for the potent and selective inhibition of casein kinase 1 epsilon.
Long, A.M., Zhao, H., Huang, X.(2012) J Med Chem 55: 10307-10311
- PubMed: 23106386
- DOI: https://doi.org/10.1021/jm301336n
- Primary Citation of Related Structures:
4HNF, 4HNI, 4HOK - PubMed 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.
Organizational Affiliation:
Department of Molecular Structure and Characterization, Amgen Inc., 360 Binney Street, Cambridge, Massachusetts 02142, USA.
