Role of Conserved Serine Residues in the Interaction of Agonists with D3 Dopamine Receptors

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Abstract
To understand the role of conserved serine residues in the fifth transmembrane domain (Ser192, Ser193, and Ser196) of the D3 dopamine receptor, these have been mutated individually to alanine, and the ligand binding properties of the mutant receptors have been evaluated. The mutations had little or no effect on the binding of the antagonist spiperone and the agonist quinpirole, indicating that the overall conformation of the receptor was unaffected. The binding of dopamine and 7‐hydroxydipropylaminotetralin, agonists containing hydroxyl groups, was, however, of lower affinity for the Ser192 mutation but unaffected by the other mutations (Ser193 and Ser196). Therefore, for the agonists tested, the hydroxyl groups interact exclusively with Ser192.