NMR studies on the flexibility of nucleoside diphosphate kinase.

Y. Xu (1) , Anne Lecroisey (2) , Michel Véron (3) , Joël Janin (1) , Muriel Delepierre (2)

1 LEBS - Laboratoire d'enzymologie et biochimie structurales
2 Résonance Magnétique Nucléaire
3 Biochimie cellulaire

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.

Y. Xu, Anne Lecroisey, Michel Véron, Joël Janin, Muriel Delepierre. NMR studies on the flexibility of nucleoside diphosphate kinase.. Proteins - Structure, Function and Bioinformatics, 1997, 28 (2), pp.150-2. ⟨10.1002/(SICI)1097-0134(199706)28:2⟩. ⟨pasteur-00372794⟩