1hiy | pdb_00001hiy
BINDING OF NUCLEOTIDES TO NDP KINASE
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Overview
The source of affinity for substrates of human nucleoside diphosphate, (NDP) kinases is particularly important in that its knowledge could be, used to design more effective antiviral nucleoside drugs (e.g., AZT). We, carried out a microcalorimetric study of the binding of enzymes from two, organisms to various nucleotides. Isothermal titration calorimetry has, been used to characterize the binding in terms of Delta G degrees, Delta H, degrees and Delta S degrees. Thermodynamic parameters of the interaction, of ADP with the hexameric NDP kinase from Dictyostelium discoideum and, with the tetrameric enzyme from Myxococcus xanthus, at 20 degrees C, were, similar and, in both cases, binding was enthalpy-driven. The interactions, of ADP, 2'deoxyADP, GDP, and IDP with the eukaryotic enzyme ... [(full description)]
About this Structure
1HIY is a [Single protein] structure of sequence from [Dictyostelium discoideum] with 3AN as [ligand]. Active as [Nucleoside-diphosphate kinase], with EC number [2.7.4.6]. Structure known Active Sites: AC1, AC2 and AC3. Full crystallographic information is available from [OCA].
Reference
Binding of nucleotides to nucleoside diphosphate kinase: a calorimetric study., Cervoni L, Lascu I, Xu Y, Gonin P, Morr M, Merouani M, Janin J, Giartosio A, Biochemistry. 2001 Apr 17;40(15):4583-9. PMID:11294625
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