Structural insight into human CK2α in complex with the potent inhibitor ellagic acid

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.

2.35 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 as PowerPoint slide