4HNI

crystal structure of ck1e in complex with PF4800567

Summary for 4HNI

• Entry DOI: 10.2210/pdb4hni/pdb
• Related: 4HNK 4HOK
• Descriptor: Casein kinase I isoform epsilon, 3-[(3-chlorophenoxy)methyl]-1-(tetrahydro-2H-pyran-4-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ck1e, kinase, inhibitor, pf4800567, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 70215.41

Authors

Huang, X.,Long, A.M.,Zhao, H. (deposition date: 2012-10-19, release date: 2012-11-14, Last modification date: 2024-02-28)

Primary citation

Long, A.M.,Zhao, H.,Huang, X.
Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.
J.Med.Chem., 55:10307-10311, 2012

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.

PubMed: 23106386
DOI: 10.1021/jm301336n

Experimental method

X-RAY DIFFRACTION (2.74 Å)