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Systematic Investigation of Non-Nucleoside Inhibitors of HIV-1 Reverse Transcriptase (NNRTIs)

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Summary.

The 44 crystal structures of NNRTIs complexed with HIV-1 reverse transcriptase (RT) have been analyzed in detail especially the orientation geometries and the distances between inhibitor molecules and surrounding amino acids. In general, various NNIs bind to the same region of the HIV-1 RT in the palm subdomain of p66, but subtle differences in individual interactions between RT and its inhibitors can be detected by comparison of all structures in this study.

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Authors and Affiliations

  1. Research Institute of Molecular Pathology, 1030, Vienna, Austria

    Anton Beyer

  2. Department of Common and Graduate Studies, Sirindhorn International Institute of Technology (SIIT), Thammasat University, P.O. Box 22, 12121, Thammasat Rangsit Post Office, Pathumthani, Thailand

    Luckhana Lawtrakul

  3. Department of Chemistry, Faculty of Science, Kasetsart University, 10900, Bangkok, Thailand

    Supa Hannongbua

  4. Institute of Theoretical Chemistry and Structural Biology, 1090, Vienna, Austria

    Peter Wolschann

Authors
  1. Anton Beyer
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  2. Luckhana Lawtrakul
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  3. Supa Hannongbua
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  4. Peter Wolschann
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Corresponding authors

Correspondence to Anton Beyer or Luckhana Lawtrakul.

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Beyer, A., Lawtrakul, L., Hannongbua, S. et al. Systematic Investigation of Non-Nucleoside Inhibitors of HIV-1 Reverse Transcriptase (NNRTIs). Monatshefte für Chemie 135, 1047–1059 (2004). https://doi.org/10.1007/s00706-004-0173-y

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  • DOI: https://doi.org/10.1007/s00706-004-0173-y

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