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Structural step forward for NHEJ
Cell Research ( IF 44.1 ) Pub Date : 2017-11-06 , DOI: 10.1038/cr.2017.119
Go Watanabe , Michael R Lieber , Dewight Williams

In a recent paper published in Cell Research, a cryo-EM structure reveals the interface between DNA-PKcs and the Ku70/80:DNA complex, together forming the DNA-dependent protein kinase holoenzyme in non-homologous DNA end joining. Insight from this structure suggests how an allosteric rearrangement of DNA-PKcs driven by Ku70/80:DNA binding regulates kinase activity in this largest member of a family of structurally homologous phosphoinositide 3-kinase-related protein kinases that includes mTOR, ATR, and ATM.

中文翻译:

NHEJ的结构性进步

在最近发表在《细胞研究》上的一篇论文中,一种低温电磁结构揭示了DNA-PKcs与Ku70 / 80:DNA复合体之间的界面,共同在非同源DNA末端连接中形成了DNA依赖性蛋白激酶全酶。从此结构的洞察力表明,由Ku70 / 80:DNA结合驱动的DNA-PKcs的变构重排如何调节结构同源的磷酸肌醇3激酶相关蛋白激酶家族(包括mTOR,ATR和ATM)中这个最大成员的激酶活性。
更新日期:2017-11-06
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