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Title: Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon

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.

Authors:
 [1];  [1];  [1]
  1. Amgen Inc., Cambridge, MA (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1056698
Resource Type:
Journal Article
Journal Name:
Journal of Medicinal Chemistry
Additional Journal Information:
Journal Volume: 55; Journal Issue: 22; Journal ID: ISSN 0022-2623
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Long, Alexander M., Zhao, Huilin, and Huang, Xin. Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon. United States: N. p., 2012. Web. doi:10.1021/jm301336n.
Long, Alexander M., Zhao, Huilin, & Huang, Xin. Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon. United States. doi:10.1021/jm301336n.
Long, Alexander M., Zhao, Huilin, and Huang, Xin. Mon . "Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon". United States. doi:10.1021/jm301336n.
@article{osti_1056698,
title = {Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon},
author = {Long, Alexander M. and Zhao, Huilin and Huang, Xin},
abstractNote = {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.},
doi = {10.1021/jm301336n},
journal = {Journal of Medicinal Chemistry},
issn = {0022-2623},
number = 22,
volume = 55,
place = {United States},
year = {2012},
month = {10}
}