Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site

Chem Biol. 1999 May;6(5):R137-46. doi: 10.1016/s1074-5521(99)80071-4.

Abstract

Comparison of the recently solved structure of HIV-1 reverse transcriptase (RT)-DNA-dNTP ternary complex with the previously solved structure of RT-DNA binary complex suggests mechanisms by which the HIV-1 RT becomes resistant to nucleoside-analog inhibitors, drugs currently used in the treatment of AIDS.

Publication types

  • Review

MeSH terms

  • Anti-HIV Agents / chemistry
  • Anti-HIV Agents / metabolism
  • Binding Sites
  • DNA, Viral / chemistry*
  • DNA, Viral / metabolism
  • DNA, Viral / physiology
  • Deoxyadenine Nucleotides / chemistry*
  • Deoxyadenine Nucleotides / metabolism
  • Deoxyguanine Nucleotides / chemistry*
  • Deoxyguanine Nucleotides / metabolism
  • Forecasting
  • HIV Reverse Transcriptase / antagonists & inhibitors
  • HIV Reverse Transcriptase / chemistry*
  • HIV Reverse Transcriptase / genetics
  • HIV Reverse Transcriptase / metabolism
  • Macromolecular Substances
  • Models, Molecular

Substances

  • Anti-HIV Agents
  • DNA, Viral
  • Deoxyadenine Nucleotides
  • Deoxyguanine Nucleotides
  • Macromolecular Substances
  • deoxyguanosine triphosphate
  • HIV Reverse Transcriptase
  • 2'-deoxyadenosine triphosphate