Owing to their crucial role in the modulation of cell pathways, protein kinases are important targets for several human diseases, including but not limited to cancer. The classic approach of targeting the ATP active site has recently come up against selectivity issues, which can be considerably reduced by following an allosteric modulation approach. Being closely related to protein kinase inactivation, allosteric targeting via displacement of the conserved structural αC helix enables a direct and specific modulation mechanism. A structure-based survey of the allosteric regulation of αC helix conformation in various kinase families is provided, highlighting key allosteric pockets and modulation mechanisms that appear to be more broadly conserved than was previously thought.

译文

蛋白激酶由于其在调节细胞途径中的关键作用,因此成为多种人类疾病(包括但不限于癌症)的重要靶标。靶向ATP活性位点的经典方法最近遇到了选择性问题,通过采用变构调节方法可以大大降低选择性。与蛋白激酶失活密切相关,通过置换保守结构αC螺旋的变构靶向可实现直接和特异性的调节机制。提供了对各种激酶家族中αC螺旋构象的变构调节的基于结构的调查,着重指出了关键的变构口袋和调节机制,它们似乎比以前认为的更为保守。

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