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Quantitative Structural Rearrangement of HIV-1 Reverse Transcriptase on Binding to Non-Nucleoside Inhibitors

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Summary.

The crystal structures of HIV-1 reverse transcriptase (RT) and some of its inhibitor complexes have been compared quantitatively with respect to backbone and side chain dihedral angles. Furthermore distances between inhibitor molecules and surrounding amino acids have been analyzed in detail. The calculation of the conformation for all structures allows us to determine quantitative structural changes of HIV-1 RT on binding to NNIs or to RNA/DNA.

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Authors and Affiliations

  1. 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

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

    Anton Beyer

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

Correspondence to Luckhana Lawtrakul or Anton Beyer.

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Lawtrakul, L., Beyer, A., Hannongbua, S. et al. Quantitative Structural Rearrangement of HIV-1 Reverse Transcriptase on Binding to Non-Nucleoside Inhibitors. Monatshefte für Chemie 135, 1033–1046 (2004). https://doi.org/10.1007/s00706-004-0172-z

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  • DOI: https://doi.org/10.1007/s00706-004-0172-z

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