Structural highlights
Publication Abstract from PubMed
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.
Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon.,Long AM, Zhao H, Huang X J Med Chem. 2012 Nov 9. PMID:23106386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Long AM, Zhao H, Huang X. Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon. J Med Chem. 2012 Nov 9. PMID:23106386 doi:http://dx.doi.org/10.1021/jm301336n
