Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation

Nat Struct Biol. 1997 Aug;4(8):601-4. doi: 10.1038/nsb0897-601.
No abstract available

Publication types

  • Comparative Study
  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computer Simulation
  • Crystallography
  • Dideoxynucleotides
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Motion
  • Nucleoside-Phosphate Kinase / chemistry*
  • Nucleoside-Phosphate Kinase / metabolism
  • Phosphorylation
  • Prodrugs / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Substrate Specificity
  • Thymidine Monophosphate / chemistry*
  • Thymidine Monophosphate / metabolism
  • Thymine Nucleotides / chemistry*
  • Thymine Nucleotides / metabolism
  • Zidovudine / analogs & derivatives*
  • Zidovudine / chemistry
  • Zidovudine / metabolism*

Substances

  • Dideoxynucleotides
  • Prodrugs
  • Thymine Nucleotides
  • 3'-azido-3'-deoxythymidine 5'phosphate
  • Thymidine Monophosphate
  • Zidovudine
  • Nucleoside-Phosphate Kinase
  • dTMP kinase