| Literature DB >> 28925388 |
Go Watanabe1, Michael R Lieber1, Dewight Williams2.
Abstract
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.Entities:
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Year: 2017 PMID: 28925388 PMCID: PMC5674156 DOI: 10.1038/cr.2017.119
Source DB: PubMed Journal: Cell Res ISSN: 1001-0602 Impact factor: 25.617