Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant.

@article{Lindberg2002StructuralBF,
  title={Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant.},
  author={Jimmy Lindberg and Snaevar Sigurdsson and Seved L{\"o}wgren and Hans O. Andersson and Christer Sahlberg and Rolf Nor{\'e}en and Kerstin Fridborg and Hong Zhang and Torsten Unge},
  journal={European journal of biochemistry},
  year={2002},
  volume={269 6},
  pages={
          1670-7
        }
}
The K103N substitution is a frequently observed HIV-1 RT mutation in patients who do not respond to combination-therapy. The drugs Efavirenz, MSC194 and PNU142721 belong to the recent generation of NNRTIs characterized by an improved resistance profile to the most common single point mutations within HIV-1 RT, including the K103N mutation. In the present study we present structural observations from Efavirenz in complex with wild-type protein and the K103N mutant and PNU142721 and MSC194 in… Expand
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The HIV-1 Reverse Transcriptase M184I Mutation Enhances the E138K-Associated Resistance to Rilpivirine and Decreases Viral Fitness
TLDR
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HIV-1 reverse transcriptase connection subdomain mutations involved in resistance to approved non-nucleoside inhibitors.
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