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K65R and K65A substitutions in HIV-1 reverse transcriptase enhance polymerase fidelity by decreasing both dNTP misinsertion and mispaired primer extension efficiencies
The Lys65 residue, in the fingers domain of HIV reverse transcriptase (RT), interacts in a sequence independent fashion with the incoming dNTP. Previously, we showed that a 5 amino acid deletion spanning Lys65 and a K65A substitution both enhanced the fidelity of dNTP insertion. We hypothesized that...
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| Главные авторы: | , , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2010
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2925049/ https://ncbi.nlm.nih.gov/pubmed/20538005 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2010.06.001 |
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