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Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs)

机译：DNA依赖性蛋白激酶催化亚基（DNA-PKcs）的三维结构和调控

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摘要

DNA-PKcs is a large PI3-kinase-related protein kinase (PIKK) that plays a central role in DNA double-strand break (DSB) repair via nonhomologous end joining. Using cryo-electron microscopy we have now generated a similar to13 Angstrom three-dimensional map of DNA-PKcs, revealing the overall architecture and topology of the 4128 residue polypeptide chain and allowing location of domains. The highly conserved C-terminal PIKK catalytic domain forms a central structure from which FAT and FATC domains protrude. Conformational changes observed in these domains on DNA binding suggest that they transduce DNA-induced conformational changes to the catalytic core and regulate kinase activity. The N-terminal segments form long curved tubular-shaped domains based on helical repeats to create interacting surfaces required for macromolecular assembly. Comparison of DNA-PKcs with another PIKK DNA repair factor, ATM, defines a common architecture for this important protein family.
机译：DNA-PKcs是一种大型的PI3激酶相关蛋白激酶（PIKK），通过非同源末端连接在DNA双链断裂（DSB）修复中起着核心作用。现在，使用冷冻电子显微镜，我们已经生成了类似于DNA PKcs的13埃三维图，揭示了4128个残基多肽链的整体结构和拓扑，并允许对结构域进行定位。高度保守的C末端PIKK催化结构域形成FAT和FATC结构域从其突出的中心结构。在这些区域上观察到的与DNA结合的构象变化表明它们将DNA诱导的构象变化转化为催化核心并调节激酶活性。 N末端部分基于螺旋重复序列形成长的弯曲管状区域，以产生大分子组装所需的相互作用表面。 DNA-PKcs与另一种PIKK DNA修复因子ATM的比较为该重要的蛋白质家族定义了通用的体系结构。

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