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• W2020631657 endingPage "2309" @default.
• W2020631657 startingPage "2301" @default.
• W2020631657 abstract "The selection of drug resistant viruses is a major problem in efforts to combat HIV and AIDS, hence, new compounds are required. We report crystal structures of wild-type and mutant HIV-1 RT with bound non-nucleoside (NNRTI) GW420867X, aimed at investigating the basis for its high potency and improved drug resistance profile compared to the first-generation drug nevirapine. GW420867X occupies a smaller volume than many NNRTIs, yet accesses key regions of the binding pocket. GW420867X has few contacts with Tyr188, hence, explaining the small effect of mutating this residue on inhibitor-binding potency. In a mutated NNRTI pocket, GW420867X either remains in a similar position compared to wild-type (RT(Leu100Ile) and RT(Tyr188Cys)) or rearranges within the pocket (RT(Lys101Glu)). For RT(Leu100Ile), GW420867X does not shift position, in spite of forming different side-chain contacts. The small bulk of GW420867X allows adaptation to a mutated NNRTI binding site by repositioning or readjustment of side-chain contacts with only small reductions in binding affinity." @default.
• W2020631657 created "2016-06-24" @default.
• W2020631657 creator A5002792519 @default.
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• W2020631657 date "2007-04-19" @default.
• W2020631657 modified "2023-10-07" @default.
• W2020631657 title "Relationship of Potency and Resilience to Drug Resistant Mutations for GW420867X Revealed by Crystal Structures of Inhibitor Complexes for Wild-Type, Leu100Ile, Lys101Glu, and Tyr188Cys Mutant HIV-1 Reverse Transcriptases" @default.
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• W2020631657 doi "https://doi.org/10.1021/jm061117m" @default.
• W2020631657 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17441703" @default.
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