Exploring human 5HT1A/2A receptor through Homology modeling and flexible docking studies for the binding hotspot of substituted 2,4-imidazolidinedione and Oxazolidinedione derivatives



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. The docking scores that were generated are correlated with the in-vivo affinity data that had already been collected. When combined with a homology model of 5HT1A/2A, the GLIDE docking approach was based on a template for 2-adrenergic receptors. 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.



The influence of structure and hydrophobic properties of aryl moiety on binding affinities was discussed and a model for ligand binding in the hydrophobic part of the binding site was proposed.



These studies have provided useful insight into the possible binding modes of heteroaryl ligands and on the path by which they are giving their particular action at human 5-HT1A/2A receptor, which will give a significant preface in search of potent ligand for 5-HT1A/2A receptor.
