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• W2030793556 abstract "The interactions of the NK 1 receptor with peptide agonists or nonpeptide antagonists have been investigated by site-directed mutagenesis and computer modeling. At least 10 residues in the extracellular and transmembrane regions of the receptor are required for the binding of many peptide agonists. The C-terminal amide of peptide agonists is likely to be bound near Asn-85. Residues likely to be involved in the subsequent receptor activation include Glu-78 and Tyr-205. The binding site for nonpeptide antagonists can be defined by at least five residues in transmembrane helices 4–7, and primary contacts between key residues and quinuclidine antagonists have been assigned based on CP-96,345 and its analogs. Analyses of the wild-type and mutant NK 1 and NK 2 receptors, intact and truncated peptides, and various antagonists suggest that the agonist and antagonist binding sites overlap spatially, even though agonists and antagonists do not interact with the same set of residues on the receptor. Mapping the ligand binding site not only allows us to better understand the ligand–receptor interaction and antagonism but also leads to a refined three-dimensional model of the NK 1 receptor.Key words: receptor, substance P, agonist, antagonist, mutagenesis." @default.
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• W2030793556 date "1995-07-01" @default.
• W2030793556 modified "2023-09-23" @default.
• W2030793556 title "Mutational analysis of neurokinin receptor function" @default.
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• W2030793556 doi "https://doi.org/10.1139/y95-118" @default.
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