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Viruses. 2014 Oct 23;6(10):4080-94. doi: 10.3390/v6104080.

The lysine 65 residue in HIV-1 reverse transcriptase function and in nucleoside analog drug resistance.

Author information

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. scott.garforth@einstein.yu.edu.
  • 2Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. vinayaka.prasad@einstein.yu.edu.

Abstract

Mutations in HIV-1 reverse transcriptase (RT) that confer nucleoside analog RT inhibitor resistance have highlighted the functional importance of several active site residues (M184, Q151 and K65) in RT catalytic function. Of these, K65 residue is notable due to its pivotal position in the dNTP-binding pocket, its involvement in nucleoside analog resistance and polymerase fidelity. This review focuses on K65 residue and summarizes a substantial body of biochemical and structural studies of its role in RT function and the functional consequences of the K65R mutation.

PMID:
25341667
PMCID:
PMC4213578
DOI:
10.3390/v6104080
[PubMed - in process]
Free PMC Article
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