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Merck

Structural insight into human CK2alpha in complex with the potent inhibitor ellagic acid.

Bioorganic & medicinal chemistry letters (2009-05-06)
Yusuke Sekiguchi, Tetsuko Nakaniwa, Takayoshi Kinoshita, Isao Nakanishi, Kazuo Kitaura, Akira Hirasawa, Gozoh Tsujimoto, Toshiji Tada
RESUMO

We determined the 2.35-A crystal structure of a human CK2 catalytic subunit (referred to as CK2alpha complexed with the ATP-competitive, potent CK2 inhibitor ellagic acid. The inhibitor binds to CK2alpha with a novel binding mode, including water-mediated hydrogen bonds. This structural information may support discovery of potent CK2 inhibitors.

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Sigma-Aldrich
Ellagic acid, ≥95% (HPLC), powder, from tree bark
Sigma-Aldrich
Apigenin, ≥95.0% (HPLC)
Sigma-Aldrich
5,6-Dichlorobenzimidazole 1-β-D-ribofuranoside
Sigma-Aldrich
Emodin, from Frangula bark, ≥90% (HPLC)