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

被引:101
作者
Sarafianos, SG
Das, K
Ding, JP
Boyer, PL
Hughes, SH
Arnold, E
机构
[1] Rutgers State Univ, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA
[2] Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA
[3] NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Frederick, MD 21702 USA
来源
CHEMISTRY & BIOLOGY | 1999年 / 6卷 / 05期
关键词
D O I
10.1016/S1074-5521(99)80071-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:R137 / R146
页数:10
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