Selective inhibitors of protein kinase CK2 with significant cytotoxicity on tumor cells based on a 2-aminothiazole scaffold were described recently. Here, these studies are supplemented with representative CK2α/CK2α′ complex structures. They reveal that the 2-aminothiazole-based inhibitors occupy the ATP cavity, whereas preliminary data had indicated an allosteric binding site. The crystal structure findings are corroborated by subsequent enzyme kinetic studies; their atomic-resolution quality provides the basis for future optimization of these promising CK2 inhibitors.

中文翻译：

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所选2-氨基噻唑化合物对蛋白激酶CK2抑制能力的结构和机理基础。

最近描述了基于2-氨基噻唑支架的对肿瘤细胞具有明显细胞毒性的蛋白激酶CK2的选择性抑制剂。在这里，这些研究补充了代表性的CK2α/CK2α'复合结构。他们发现，基于2-氨基噻唑的抑制剂占据了ATP腔，而初步数据表明了变构结合位点。随后的酶动力学研究证实了晶体结构的发现。它们的原子分辨率质量为这些有前途的CK2抑制剂的未来优化提供了基础。