Search for: [Abstract = "a\-aminobutyric acid \(GAT\-1, BGT\-1, GAT\-2, GAT\-3\) and glycine \(GlyT\-1, GlyT\-2\) using molecular modelling methods. In the course of the study, a diverse pool of homology models of each transporter was generated. From this pool, the final models were selected which, according to the assessment of the applied bioinformatic tools, best reflected the actual structure of the proteins and explained the structure\-activity relationship for the ligands docked into their binding sites. The constructed models allowed for a comparative analysis of the spatial structure of all types of GABA and glycine transporters, along with a comparison with other related proteins of known structure. The analysis focused on the structure of the binding sites, including the identification of the amino acids that have the greatest influence on the properties of specific transporters. The indicated differences were reflected in the results of the molecular docking of the reference ligands of each transporter. The stability of the binding modes obtained in the docking studies was verified by molecular dynamics simulations. Additionally, in some analyses, calculations of the free energy of ligand binding were carried out to indicate a more favourable binding mode. In silico studies show that the carboxyl group of GABA transporter inhibitors with amino acid structure is located at the main bindin"]

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