| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1373714 | Bioorganic & Medicinal Chemistry Letters | 2009 | 4 Pages |
Abstract
We determined the 2.35-Å crystal structure of a human CK2 catalytic subunit (referred to as CK2α complexed with the ATP-competitive, potent CK2 inhibitor ellagic acid. The inhibitor binds to CK2α with a novel binding mode, including water-mediated hydrogen bonds. This structural information may support discovery of potent CK2 inhibitors.
Graphical abstract2.35 Å X-ray crystal structure reveals that ellagic acid binds to human CK2α with a novel binding mode including four water mediated interactions and induces a specific conformation at His160.Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Yusuke Sekiguchi, Tetsuko Nakaniwa, Takayoshi Kinoshita, Isao Nakanishi, Kazuo Kitaura, Akira Hirasawa, Gozoh Tsujimoto, Toshiji Tada,