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

  1. Author:
    Boyer, P. L.
    Sarafianos, S. G.
    Arnold, E.
    Hughes, S. H.

  2. Author Address

    Hughes SH NCI, HIV Drug Resistance Program, Adv Biosci Labs, Basic Res Program,Frederick Canc Res & Dev Ctr POB B,Bldg 539,Room 130A Ft Detrick, MD 21702 USA NCI, HIV Drug Resistance Program, Adv Biosci Labs, Basic Res Program,Frederick Canc Res & Dev Ctr Ft Detrick, MD 21702 USA Rutgers State Univ, Ctr Adv Biotechnol & Med Piscataway, NJ 08854 USA Rutgers State Univ, Dept Chem Piscataway, NJ 08854 USA
    1. Year: 2000
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 97
    2. 7
    3. Pages: 3056-3061
  4. Type of Article: Article
  1. Abstract:

    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-215-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. [References: 34]

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