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.
Original language | English (US) |
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Pages (from-to) | 4080-4094 |
Number of pages | 15 |
Journal | Viruses |
Volume | 6 |
Issue number | 10 |
DOIs | |
State | Published - Oct 23 2014 |
Keywords
- HIV-1 drug resistance
- HIV-1 reverse transcriptase
- K65R mutation
- NRTI analog resistance
- Polymerase fidelity
- Reverse transcriptase function
ASJC Scopus subject areas
- Infectious Diseases
- Virology