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

DNA repair | Mar 7, 2006

http://www.ncbi.nlm.nih.gov/pubmed/16388993

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 RIS Download

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