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，较好的结果说明该模型是可靠的 Using the three-dimensional crystal structure of bacteriorhodopsin as a template, the three-dimensional structure of seven α-helical peptides in the transmembrane region of dopamine D2 receptor was predicted. Based on the experimental data of site-directed mutagenesis and the predicted three-dimensional structure of the receptor, it was confirmed that the ligand of the agonist ligand consists of twelve amino acid residues, such as Asp86, Ser141 and Ser144. In order to calibrate and test the resulting model, the correlation between logIC50 and binding energy Eb was analyzed by a set of rigid, flexible agonist and receptor docking (DOCK) respectively. The good results show that the model is reliable