Analysis of mutations at positions 115 and 116 in the dNTP binding site of HIV-1 reverse transcriptase

Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3056-61. doi: 10.1073/pnas.97.7.3056.


We have examined amino acid substitutions at residues 115 and 116 in the reverse transcriptase (RT) of HIV-1. A number of properties were examined, including polymerization and processivity on both DNA and RNA templates, strand displacement, ribonucleotide misincorporation, and resistance to nucleoside analogs. The RT variants Tyr-115-Phe and Phe-116-Tyr are similar to wild-type HIV-1 RT in most, but not all, respects. In contrast, the RT variant Tyr-115-Val is significantly impaired in polymerase activity compared with wild-type RT; however, Tyr-115-Val is able to incorporate ribonucleotides as well as deoxyribonucleotides during polymerization and is resistant to a variety of nucleoside analogs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Deoxyribonucleotides / genetics
  • Deoxyribonucleotides / metabolism*
  • Drug Resistance, Microbial
  • HIV Reverse Transcriptase / chemistry
  • HIV Reverse Transcriptase / genetics
  • HIV Reverse Transcriptase / metabolism*
  • HIV-1 / drug effects
  • HIV-1 / enzymology
  • Kinetics
  • Reverse Transcriptase Inhibitors / pharmacology


  • Deoxyribonucleotides
  • Reverse Transcriptase Inhibitors
  • HIV Reverse Transcriptase