Udier-Blagović Marina, Tirado-Rives Julian, Jorgensen William L
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
J Med Chem. 2004 Apr 22;47(9):2389-92. doi: 10.1021/jm0303507.
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 wild-type 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.
通过蒙特卡洛/自由能微扰计算研究了HIV-1逆转录酶（RT）的K103N突变对依非韦伦类似物活性的影响。相对折叠抗性能量表明，依非韦伦以与野生型酶相似的方式与K103N RT结合。喹唑啉酮对突变酶性能的改善归因于在配体和Glu138之间形成了一个更优化的氢键网络，其中有桥连水分子。
