title: DNA repair gets physical: mapping an XPA-binding site on ERCC1.
abstract: Two recent reports provide new physical information on how the XPA protein recruits the ERCC1-XPF heterodimer to the site of damage during the process of mammalian nucleotide excision repair (NER). Using chemical shift perturbation NMR experiments, the contact sites between a central fragment of ERCC1 and an XPA fragment have been mapped. While both studies agree with regard to the XPA-binding site, they differ on whether the ERCC1-XPA complex can simultaneously bind DNA. These studies have important implications for both the molecular process and the design of potential inhibitors of NER.
authors.affiliation: Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, United States.
authors.forename: Deborah L
authors.initials: DL
authors.lastname: Croteau
authors.forename: Ye
authors.initials: Y
authors.lastname: Peng
authors.forename: Bennett
authors.initials: B
authors.lastname: Van Houten
mesh_terms: D001665:Binding Sites / Q000235:genetics; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004720:Endonucleases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051760:Xeroderma Pigmentosum Group A Protein / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; C497314:XPA protein, human; D051760:Xeroderma Pigmentosum Group A Protein; C071447:ERCC1 protein, human; D004720:Endonucleases