The Lysine 65 Residue in HIV-1 Reverse Transcriptase Function and in Nucleoside Analog Drug Resistance
- Resource Type
- Authors
- Chisanga Lwatula; Vinayaka R. Prasad; Scott J. Garforth
- Source
- Viruses
Viruses, Vol 6, Iss 10, Pp 4080-4094 (2014)
- Subject
- Models, Molecular
reverse transcriptase function
Lysine
lcsh:QR1-502
Mutation, Missense
K65R mutation
Review
lcsh:Microbiology
03 medical and health sciences
Residue (chemistry)
Catalytic Domain
polymerase fidelity
Virology
Drug Resistance, Viral
Humans
Polymerase
030304 developmental biology
0303 health sciences
biology
030306 microbiology
K65r mutation
Active site
HIV Reverse Transcriptase
Reverse transcriptase
3. Good health
Infectious Diseases
Amino Acid Substitution
Biochemistry
HIV-1
biology.protein
Reverse Transcriptase Inhibitors
HIV-1 reverse transcriptase
HIV-1 drug resistance
Nucleoside
NRTI analog resistance
Function (biology)
- Language
- ISSN
- 1999-4915
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.