Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site

S G Sarafianos; K Das; J Ding; P L Boyer; S H Hughes; E Arnold

doi:10.1016/s1074-5521(99)80071-4

Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site

Chem Biol. 1999 May;6(5):R137-46. doi: 10.1016/s1074-5521(99)80071-4.

Authors

S G Sarafianos¹, K Das, J Ding, P L Boyer, S H Hughes, E Arnold

Affiliation

¹ Center for Advanced Biotechnology and Medicine (CABM), Rutgers University Chemistry Department, 679 Hoes Lane, Piscataway, NJ 08854-5638, USA.

PMID: 10322129
DOI: 10.1016/s1074-5521(99)80071-4

Abstract

Comparison of the recently solved structure of HIV-1 reverse transcriptase (RT)-DNA-dNTP ternary complex with the previously solved structure of RT-DNA binary complex suggests mechanisms by which the HIV-1 RT becomes resistant to nucleoside-analog inhibitors, drugs currently used in the treatment of AIDS.

Publication types

Review

MeSH terms

Anti-HIV Agents / chemistry
Anti-HIV Agents / metabolism
Binding Sites
DNA, Viral / chemistry*
DNA, Viral / metabolism
DNA, Viral / physiology
Deoxyadenine Nucleotides / chemistry*
Deoxyadenine Nucleotides / metabolism
Deoxyguanine Nucleotides / chemistry*
Deoxyguanine Nucleotides / metabolism
Forecasting
HIV Reverse Transcriptase / antagonists & inhibitors
HIV Reverse Transcriptase / chemistry*
HIV Reverse Transcriptase / genetics
HIV Reverse Transcriptase / metabolism
Macromolecular Substances
Models, Molecular

Substances

Anti-HIV Agents
DNA, Viral
Deoxyadenine Nucleotides
Deoxyguanine Nucleotides
Macromolecular Substances
deoxyguanosine triphosphate
HIV Reverse Transcriptase
2'-deoxyadenosine triphosphate