Abstract: A model of dopamine D2 receptor transmembrane helices was constructed using the bacteriorhodopsin X-ray coordinates as a template. Based on the information from sitedirected mutagenesis, the binding pocket, including nine amino acid residues besides indispensable Asp 86, Ser 141 and Ser 144 residues, was defined. In order to rectify the 3D-structure of dopamine D2 receptor and test the binding sites of the receptor agonists, two sets of dopamine D2 receptor agonists (one is rigid, the other is flexible) were selected for docking. A result of good correlation between-logIC₅₀ and binding energy E_b indicated that the predicted model is reliable for the investigation of the receptorligand interaction and design of new active molecules.