期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 47, 期 9, 页码 2389-2392出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm0303507
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资金
- NIAID NIH HHS [AI44616] Funding Source: Medline
The effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efavirenz analogues was studied via Monte Carlo/free energy perturbation calculations. The relative fold resistance energies indicate that efavirenz binds to K103N RT in a manner similar to the wildtype enzyme. The improved performance of the quinazolinones against the mutant enzyme is attributed to formation of a more optimal hydrogen-bonding network with bridging water molecules between the ligands and Glu138.
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