[摘要]：We determined the 2.35-angstrom crystal structure of a human CK2 catalytic subunit (referred to as CK2 alpha complexed with the ATP-competitive, potent CK2 inhibitor ellagic acid. The inhibitor binds to CK2 alpha with a novel binding mode, including water-mediated hydrogen bonds. This structural information may support discovery of potent CK2 inhibitors. (C) 2009 Elsevier Ltd. All rights reserved.
