摘要
以细菌视紫红质（ｂａｃｔｅｒｉｏｒｈｏｄｏｐｓｉｎ）的三维晶体结构为模板，预测了多巴胺Ｄ２受体跨膜区的七个α螺旋肽段的三维结构。根据定点突变实验数据以及预测的受体三维结构，确定了激动剂配体结合腔由Ａｓｐ８６，Ｓｅｒ１４１，Ｓｅｒ１４４等十二个氨基酸残基组成。为了校正和检验所得的模型，分别以一组刚性、一组柔性的激动剂与受体对接（ＤＯＣＫ），分析ｌｏｇＩＣ５０和结合能Ｅｂ相关性。
A model of transmembrane helices of dopamine D2 receptor was constructed using the X ray coordinates of bacteriorhodopsin (BR) as a template. Based on the results from the model and the site directed mutagenesis experience, the binding pocket, including nine amino acid residues beside indispensable Asp86, Ser141 and Ser144 residues, was defined. In order to testify the 3D structure of dopamine D2 receptor and specially test the binding sites, two sets of D2 receptor agonists (one was rigid and the other flexible) were selected for docking. A good result of correlation between logIC 50 and binding energy E b indicates that the predicted model is reliable for the investigation of the receptor ligand interaction and design of new active molecules.
