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- W2023043760 endingPage "1038" @default.
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- W2023043760 abstract "Alpha2-adrenergic receptor (α2-AR) subtypes, acting mainly on the central nervous and cardiovascular systems, represent important targets for drug design, confirmed by the high number of studies published so far. Presently, only a few α2-AR subtype selective compounds are known. Using homology modeling and ligand docking, the present study analyzes the similarities and differences between binding sites, and between extracellular loops of the three subtypes of α2-ARs. Several α2-AR subtype selective ligands were docked into the active sites of the three α2-AR subtypes, key interactions between ligands and receptors were mapped, and the predicted results were compared with the available experimental data. Binding site analysis reveals a strong identity between important amino acid residues in each receptor, the very few differences being the key toward modulating selectivity of α2-AR ligands. The observed differences between binding site residues provide an excellent starting point for virtual screening of chemical databases, in order to identify potentially selective ligands for α2-ARs." @default.
- W2023043760 created "2016-06-24" @default.
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- W2023043760 date "2011-08-01" @default.
- W2023043760 modified "2023-09-27" @default.
- W2023043760 title "Structural determinants of the alpha2 adrenoceptor subtype selectivity" @default.
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- W2023043760 doi "https://doi.org/10.1016/j.jmgm.2011.04.011" @default.
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