Chau P L, Dean P M
Department of Pharmacology, University of Cambridge, U.K.
J Comput Aided Mol Des. 1994 Oct;8(5):513-25. doi: 10.1007/BF00123663.
Electrostatic interactions have always been considered an important factor governing ligand-receptor interactions. Previous work in this field has established the existence of electrostatic complementarity between the ligand and its receptor site. However, this property has not been treated rigorously, and the description remains largely qualitative. In this work, 34 data sets of high quality were chosen from the Brookhaven Protein Databank. The electrostatic complementary has been calculated between the surface potentials; complementarity is absent between adjacent or neighbouring atoms of the ligand and the receptor. There is little difference between complementarities on the total ligand surface and the interfacial region. Altering the homogeneous dielectric to distance-dependent dielectrics reduces the complementarity slightly, but does not affect the pattern of complementarity.
静电相互作用一直被视为支配配体 - 受体相互作用的一个重要因素。该领域以前的工作已经证实配体与其受体位点之间存在静电互补性。然而，这一特性尚未得到严格处理，描述仍主要是定性的。在这项工作中，从布鲁克海文蛋白质数据库中选取了34个高质量数据集。计算了表面电位之间的静电互补性；配体和受体的相邻或邻近原子之间不存在互补性。配体总表面和界面区域的互补性之间几乎没有差异。将均匀电介质改为距离依赖性电介质会使互补性略有降低，但不影响互补性模式。
