NMR spectroscopy in structure-based drug design.
NMR spectroscopy in structure-based drug design.
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DOI：
10.1016/s0958-1669(99)80008-1
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发表时间：
1999-02
影响因子：
7.7
通讯作者：
G. Roberts
中科院分区：
文献类型：
--
作者：
G. Roberts
用于研究蛋白质运动的NMR方法不断改进，在过去的一年中，已经报道了许多与药物设计相关的蛋白质-配体复合物的研究，例如，脂肪酸结合蛋白和SH 2和SH 3结构域的研究。这些研究已经开始给出蛋白质-配体复合物的结构动力学的图片，并将配体结合的动力学变化与特异性的起源联系起来。NMR在定位结合位点方面也很有价值，无论是从化学位移的变化定性，还是从弛豫效应测量的距离更精确。结合配体的构象可以为药物设计提供有用的信息，并且在过去的一年中，方法的改进使得从转移核奥弗豪瑟效应实验中获得定量信息变得更加容易。
NMR methods for the study of motion in proteins continue to improve, and a number of studies of protein–ligand complexes relevant to drug design have been reported over the past year, for example, studies of fatty-acid-binding protein and SH2 and SH3 domains. These studies have begun to give a picture of the structural dynamics of protein–ligand complexes and to relate the changes in dynamics on ligand binding to the origins of specificity. NMR is also valuable in locating binding sites, both qualitatively from changes in chemical shift and more precisely from distances measured from relaxation effects. The conformation of the bound ligand can provide useful information for drug design, and over the past year improvements in methods have made it easier to obtain quantitative information from transferred nuclear Overhauser effect experiments.