Abstract
Introduction: To obtain the binding site of a model of the human 5-HT1A/2A receptor, a series of substituted 2,4-imidazolidinediones and oxazolidinediones were subjected to flexible docking using GLIDE. Methods: The docking scores that were generated are correlated with the in-vivo affinity data that had already been collected. Results: When combined with a homology model of 5HT1A/2A, the GLIDE docking approach was based on a template for 2-adrenergic receptors. Conclusion: A model for ligand binding in the hydrophobic portion of the binding site was proposed after discussing the impact of the structure and hydrophobic characteristics of the aryl moiety on binding affinities.
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