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• W2028128317 startingPage "1093" @default.
• W2028128317 abstract "DNA double-strand breaks represent one of the most severe forms of DNA damage in mammalian cells. One pathway for repairing these breaks occurs via nonhomologous end-joining (NHEJ) and depends on XRCC4, LigaseIV, and Cernunnos, also called XLF. Although XLF stimulates XRCC4/LigaseIV to ligate mismatched and noncohesive DNA ends, the mechanistic basis for this function remains unclear. Here we report the structure of a partially functional 224 residue N-terminal fragment of human XLF. Despite only weak sequence similarity, XLF1–170 shares structural homology with XRCC41–159. However, unlike the highly extended 130 Å helical domain observed in XRCC4, XLF adopts a more compact, folded helical C-terminal region involving two turns and a twist, wrapping back to the structurally conserved N terminus. Mutational analysis of XLF and XRCC4 reveals a potential interaction interface, suggesting a mechanism for how XLF stimulates the ligation of mismatched ends." @default.
• W2028128317 created "2016-06-24" @default.
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• W2028128317 creator A5058213120 @default.
• W2028128317 creator A5059569301 @default.
• W2028128317 creator A5084899890 @default.
• W2028128317 date "2007-12-01" @default.
• W2028128317 modified "2023-10-11" @default.
• W2028128317 title "Crystal Structure of Human XLF: A Twist in Nonhomologous DNA End-Joining" @default.
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• W2028128317 doi "https://doi.org/10.1016/j.molcel.2007.10.024" @default.
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