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NMR studies on the flexibility of nucleoside diphosphate kinase
Author(s) -
Xu Y.,
Lecroisey A.,
Veron M.,
Delepierre M.,
Janin Joël
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199706)28:2<150::aid-prot3>3.0.co;2-j
Subject(s) - nucleoside diphosphate kinase , kinase , binding site , biochemistry , nucleotide , chemistry , nucleoside , stereochemistry , gene , biology , microbiology and biotechnology
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. Proteins 28:150–152, 1997. © 1997 Wiley‐Liss Inc.