Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.

@article{Ropars2011StructuralCO,
  title={Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.},
  author={Virginie Ropars and Pascal Drevet and Pierre Legrand and Sonia Baconnais and Jeremy Amram and Guilhem Faure and Jos{\'e} Antonio Alvarado M{\'a}rquez and Olivier Pi{\'e}trement and Rapha{\"e}l Gu{\'e}rois and Isabelle Callebaut and Eric le Cam and Patrick Revy and Jean-Pierre de Villartay and Jean-Baptiste Charbonnier},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 31},
  pages={12663-8}
}
Cernunnos/XLF is a core protein of the nonhomologous DNA end-joining (NHEJ) pathway that processes the majority of DNA double-strand breaks in mammals. Cernunnos stimulates the final ligation step catalyzed by the complex between DNA ligase IV and Xrcc4 (X4). Here we present the crystal structure of the X4(1-157)-Cernunnos(1-224) complex at 5.5-Å resolution… CONTINUE READING