XRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break Repair*♦

@inproceedings{Hammel2011XRCC4PI,
  title={XRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break Repair*♦},
  author={Michal Hammel and M Varela Rey and Yaping Yu and Rajam S. Mani and Scott Classen and Mona Liu and Michael E. Pique and Shujuan Fang and Brandi L. Mahaney and Michael Weinfeld and David C. Schriemer and Susan P Lees-Miller and John A. Tainer},
  booktitle={The Journal of biological chemistry},
  year={2011}
}
The XRCC4-like factor (XLF)-XRCC4 complex is essential for nonhomologous end joining, the major repair pathway for DNA double strand breaks in human cells. Yet, how XLF binds XRCC4 and impacts nonhomologous end joining functions has been enigmatic. Here, we report the XLF-XRCC4 complex crystal structure in combination with biophysical and mutational analyses to define the XLF-XRCC4 interactions. Crystal and solution structures plus mutations characterize alternating XRCC4 and XLF head domain… CONTINUE READING