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2000
Volume 1, Issue 1
  • ISSN: 2210-299X
  • E-ISSN: 2210-3007

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 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.

© 2023 The Author(s). Published by Bentham Science Publisher. This is an open access article published under CC BY 4.0 https://creativecommons.org/licenses/by/4.0/legalcode
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  • Article Type:
    Research Article
Keyword(s): Docking; GLIDE; Homology modeling; PRIME; Receptors; Schrödinger
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