Abstract
The mouse serotonin (5-HT) receptor subtype, 5-HT 7, belongs to the family of seven transmembrane G-protein-coupled receptors. To identify the structural basis for the coupling of 5-HT 7 receptor to Gα S we constructed a number of receptor mutants in which amino acid residues were either substituted or deleted from the second and third intracellular loops. Wild-type and mutant 5-HT 7 receptors were expressed in insect cells using the baculovirus vectors. Two mutant receptor species, 5-HT 7(E325G) and 5-HT 7(K327S), demonstrated markedly impaired abilities to stimulate adenylyl cyclase. The results suggest the importance of the C-terminal region of the third intracellular loop in receptor–G-protein interaction and that specific charged residues, E325 and K327, may play a critical role in this interaction.
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