Journal article
Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4
Abstract
Nonhomologous end-joining represents the major pathway used by human cells to repair DNA double-strand breaks. It relies on the XRCC4/DNA ligase IV complex to reseal DNA strands. Here we report the high-resolution crystal structure of human XRCC4 bound to the carboxy-terminal tandem BRCT repeat of DNA ligase IV. The structure differs from the homologous Saccharomyces cerevisiae complex and reveals an extensive DNA ligase IV binding interface …
Authors
Wu P-Y; Frit P; Meesala S; Dauvillier S; Modesti M; Andres SN; Huang Y; Sekiguchi J; Calsou P; Salles B
Journal
Molecular and Cellular Biology, Vol. 29, No. 11, pp. 3163–3172
Publisher
Taylor & Francis
Publication Date
June 1, 2009
DOI
10.1128/mcb.01895-08
ISSN
0270-7306
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceBinding, CompetitiveCell LineDNA Breaks, Double-StrandedDNA Ligase ATPDNA LigasesDNA RepairDNA Repair EnzymesDNA-Binding ProteinsDown-RegulationHumansMolecular Sequence DataProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRadiation ToleranceRecombination, GeneticStructural Homology, ProteinStructure-Activity Relationship