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Role of Conserved Serine Residues in the Interaction of Agonists with D 3 Dopamine Receptors
Author(s) -
Sartania Nana,
Strange Philip G.
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0722621.x
Subject(s) - spiperone , agonist , receptor , quinpirole , alanine , serine , dopamine receptor , dopamine , chemistry , transmembrane domain , mutant , endogenous agonist , biochemistry , dopamine receptor d1 , biology , stereochemistry , amino acid , endocrinology , enzyme , gene
To understand the role of conserved serine residues in thefifth transmembrane domain (Ser 192 , Ser 193 , andSer 196 ) of the D 3 dopamine receptor, these have beenmutated individually to alanine, and the ligand binding properties of themutant receptors have been evaluated. The mutations had little or no effect onthe binding of the antagonist spiperone and the agonist quinpirole, indicatingthat the overall conformation of the receptor was unaffected. The binding ofdopamine and 7‐hydroxydipropylaminotetralin, agonists containing hydroxylgroups, was, however, of lower affinity for the Ser 192 mutation butunaffected by the other mutations (Ser 193 and Ser 196 ).Therefore, for the agonists tested, the hydroxyl groups interact exclusivelywith Ser 192 .