title: NMR studies on the flexibility of nucleoside diphosphate kinase.
abstract: Human NDP kinase B, product of the nm23-H2 gene, binds DNA. It has been suggested that a helix hairpin on the protein surface, part of the nucleotide substrate binding site, could accommodate DNA binding by swinging away. The presence of flexible regions was therefore investigated by 1H NMR dynamic filtering. Although TOCSY peaks could be assigned to five residues at the N terminus of Dictyostelium NDP kinase, no flexible region was detected in the human enzyme. These data favor the idea that the protein offers different binding sites to mono- and polynucleotides.
authors.affiliation: Laboratoire d'Enzymologie et de Biologie Structurales, UPR 9063 CNRS, Gif-sur-Yvette, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Xu
authors.forename: A
authors.initials: A
authors.lastname: Lecroisey
authors.forename: M
authors.initials: M
authors.lastname: Veron
authors.forename: M
authors.initials: M
authors.lastname: Delepierre
authors.forename: J
authors.initials: J
authors.lastname: Janin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004023:Dictyostelium / Q000201:enzymology; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011522:Protons; D017386:Sequence Homology, Amino Acid
chemical_list: D011522:Protons; D009701:Nucleoside-Diphosphate Kinase