Download MendeleyStructure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.
Dore, A.S., Furnham, N., Davies, O.R., Sibanda, B.L., Chirgadze, D.Y., Jackson, S.P., Pellegrini, L., Blundell, T.L.(2006) DNA Repair (Amst) 5: 362-368
- PubMed: 16388993
- DOI: https://doi.org/10.1016/j.dnarep.2005.11.004
- Primary Citation of Related Structures:
1Z56 - PubMed Abstract:
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.
Organizational Affiliation:
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK. Andrew.Dore@icr.ac.uk
