NMR studies on the flexibility of nucleoside diphosphate kinase

✍ Scribed by Y. Xu; A. Lecroisey; M. Veron; M. Delepierre; Joël Janin

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 66 KB
• Volume: 28
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199706)28:2<150::aid-prot3>3.0.co;2-j

✦ Synopsis

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 1 H 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.