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


Doré, AS; Furnham, N; Davies, OR; Sibanda, BL; Chirgadze, DY; Jackson, SP; Pellegrini, L; Blundell, TL; (2006) Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode. DNA repair, 5 (3). pp. 362-8. ISSN 1568-7864 DOI: https://doi.org/10.1016/j.dnarep.2005.11.004

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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.<br/>

Item Type: Article
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 16388993
Web of Science ID: 236070100008
URI: http://researchonline.lshtm.ac.uk/id/eprint/2374048

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