title: DNA structures recognized by the human UV-DDB protein.
abstract: DNA recognition by the human UV-damaged DNA-binding (UV-DDB) protein was characterized. By circular permutation analyses, DNA duplexes containing the (6-4) photoproduct and the abasic site analog were found to be bent at angles of 54 degrees and 57 degrees, respectively, when they formed a complex with this protein. Although kinked NMR structures have been reported, fluorescence resonance energy transfer experiments revealed that these duplexes had no intrinsic bend. These results suggest that the UV-DDB protein binds DNA that can be bent easily at the above angle.
authors.affiliation: Department of Bioorganic Chemistry, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Mizukoshi
authors.forename: Y
authors.initials: Y
authors.lastname: Fujiwara
authors.forename: S
authors.initials: S
authors.lastname: Iwai
mesh_terms: D001483:Base Sequence; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004735:Energy Transfer; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D015183:Restriction Mapping; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
chemical_list: D004268:DNA-Binding Proteins; D009838:Oligodeoxyribonucleotides; D004247:DNA