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Unprecedented Selectivity and Structural Determinants of a New Class of Protein Kinase CK2 Inhibitors in Clinical Trials for the Treatment of Cancer

Crystal structure of human protein kinase CK2 with CX-4945, a clinical stage inhibitor for the treatment of cancer (shown with pink sticks)

Battistutta R. et al., Biochemistry 50 (39), 8478 (2011)
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CK2 is a ubiquitous, acidophilic Ser/Thr protein kinase. It has been known for a long time that kinase activity tends to be particularly high in cancer cells compared to that of their “normal” counterparts and an ample spectrum of cancer cells derived from tumors of different origin share abnormally high levels of CK2. These tumors cells have been shown to undergo apoptosis after treatments, either genetic or pharmacological, that reduce CK2 catalytic activity.
CX-4945 is the first clinical stage inhibitor of protein kinase CK2 for the treatment of cancer.
It is representative of a new class of CK2 inhibitors with Ki values in the low nanomolar range and unprecedented selectivity versus other kinases. Here we present the crystal structure of the complexes of CX-4945 and two analogues (CX-5011 and CX-5279)

with the catalytic subunit of human CK2. Consistent with their ATP-competitive mode of inhibition, all three compounds bind in the active site of CK2 (type I inhibitors).

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Unprecedented Selectivity and Structural Determinants of a New Class of Protein Kinase CK2 Inhibitors in Clinical Trials for the Treatment of Cancer; Battistutta R., Cozza G., Pierre F., Papinutto E., Lolli G., Sarno S., O’Brien S.E., Siddiqui-Jain A., Haddach M., Anderes K., Ryckman D.M., Meggio F. and Pinna L.A., Biochemistry 50 (39), 8478 (2011)
doi: 10.1021/bi2008382

Last Updated on Monday, 15 February 2016 18:10