Structural insights for producing CK2 alpha 1-specific inhibitors.
Tsuyuguchi, M., Nakaniwa, T., Hirasawa, A., Nakanishi, I., Kinoshita, T.(2020) Bioorg Med Chem Lett 30: 126837-126837
- PubMed: 31859160 
- DOI: https://doi.org/10.1016/j.bmcl.2019.126837
- Primary Citation of Related Structures:  
6L1Z, 6L20, 6L21, 6L22, 6L23, 6L24 - PubMed Abstract: 
Casein kinase 2 catalytic subunit (CK2¦Á) is classified into two subtypes CK2¦Á1 and CK2¦Á2. CK2¦Á1 is a drug discovery target, whereas CK2¦Á2 is an off-target of CK2¦Á1 inhibitors. High amino acid sequence homology between these subtypes hampers efforts to produce ATP competitive inhibitors that are highly selective to CK2¦Á1. Hematein was identified previously as a non-ATP-competitive inhibitor for CK2¦Á1, whereas this compound acts as an ATP competitive CK2¦Á2 inhibitor. Crystal structures of CK2¦Á1 and CK2¦Á2 in complex with hematein revealed distinct binding features that provide structural insights for producing CK2¦Á1-selective inhibitors.
Organizational Affiliation: 
Graduate School of Science, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan. Electronic address: tsuyuguchi13@b.s.osakafu-u.ac.jp.