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Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.

DNA ligase IV catalyses the final ligation step in the non-homologous end-joining (NHEJ) DNA repair pathway and requires interaction of the ligase with the Xrcc4 'genome-guardian', an essential NHEJ factor. Here we report the 3.9 A crystal structure of the Saccharomyces cerevisiae Xrcc4 ortholog ligase interacting factor 1 (Lif1p) complexed with the C-terminal BRCT domains of DNA ligase IV (Lig4p). The structure reveals a novel mode of protein recognition by a tandem BRCT repeat, and in addition provides a molecular basis for a human LIG4 syndrome clinical condition.

Pubmed ID: 16388993


  • DorĂ© AS
  • Furnham N
  • Davies OR
  • Sibanda BL
  • Chirgadze DY
  • Jackson SP
  • Pellegrini L
  • Blundell TL


DNA repair

Publication Data

March 7, 2006

Associated Grants

  • Agency: Wellcome Trust, Id: 064597
  • Agency: Wellcome Trust, Id: 071102

Mesh Terms

  • Amino Acid Sequence
  • BRCA1 Protein
  • Crystallization
  • Crystallography, X-Ray
  • DNA Damage
  • DNA Ligases
  • DNA Repair
  • DNA, Fungal
  • DNA-Binding Proteins
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid