Interactions of the HIV-1 reverse transcriptase 'AZT-resistant' mutant with substrates and AZT-TP.
To investigate the biochemical basis of the HIV-1 resistance to AZT we obtained the RT mutant containing four amino acid substitutions by an oligonucleotide-directed mutagenesis technique. Enzymatic properties of the wild type and mutant RTs were compared. 'AZT-resistant' mutations in RT were shown to be associated with the reduced capability of AZT-TP to block the DNA- but not RNA-directed DNA synthesis.
Pokholok
D K
DK
V.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Gudima
S O
SO
Yesipov
D S
DS
Dobrynin
V N
VN
Rechinsky
V O
VO
Kochetkov
S N
SN
D000998:Antiviral Agents / Q000494:pharmacology*; D004279:DNA, Viral / Q000096:biosynthesis; D054306:Dideoxynucleotides; D004352:Drug Resistance, Microbial / Q000235:genetics; D054303:HIV Reverse Transcriptase; D015497:HIV-1 / Q000187:drug effects / Q000201:enzymology*; D016297:Mutagenesis, Site-Directed; D012194:RNA-Directed DNA Polymerase / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D018894:Reverse Transcriptase Inhibitors; D013379:Substrate Specificity; D013942:Thymine Nucleotides / Q000494:pharmacology*; D015215:Zidovudine / Q000031:analogs & derivatives* / Q000494:pharmacology
D000998:Antiviral Agents; D004279:DNA, Viral; D054306:Dideoxynucleotides; D011994:Recombinant Proteins; D018894:Reverse Transcriptase Inhibitors; D013942:Thymine Nucleotides; D015215:Zidovudine; C052873:zidovudine triphosphate; D054303:HIV Reverse Transcriptase; D012194:RNA-Directed DNA Polymerase