Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.
Ostermann, N
Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. [electronic resource] - Journal of molecular biology Nov 2000 - 43-53 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1006/jmbi.2000.4175 doi
Anti-HIV Agents--metabolism
Binding Sites
Catalysis
Crystallography, X-Ray
Dideoxynucleotides
Enzyme Stability
Escherichia coli--enzymology
Humans
Kinetics
Models, Molecular
Mutation--genetics
Nucleoside-Phosphate Kinase--chemistry
Nucleotides--metabolism
Phosphorylation
Prodrugs--metabolism
Protein Binding
Protein Conformation
Recombinant Fusion Proteins--chemistry
Thymine Nucleotides--metabolism
Zidovudine--analogs & derivatives
Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. [electronic resource] - Journal of molecular biology Nov 2000 - 43-53 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1006/jmbi.2000.4175 doi
Anti-HIV Agents--metabolism
Binding Sites
Catalysis
Crystallography, X-Ray
Dideoxynucleotides
Enzyme Stability
Escherichia coli--enzymology
Humans
Kinetics
Models, Molecular
Mutation--genetics
Nucleoside-Phosphate Kinase--chemistry
Nucleotides--metabolism
Phosphorylation
Prodrugs--metabolism
Protein Binding
Protein Conformation
Recombinant Fusion Proteins--chemistry
Thymine Nucleotides--metabolism
Zidovudine--analogs & derivatives