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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Bibliografiset tiedot
Päätekijät: Garforth, Scott J., Domaoal, Robert A., Lwatula, Chisanga, Landau, Mark J., Meyer, Amanda J., Anderson, Karen S., Prasad, Vinayaka R.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2010
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Article
Linkit: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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