Site-directed mutagenesis, serotonin receptors

Numerous site-directed mutagenesis studies have provided a conclusive picture for the molecular interactions between the receptor-activating biogenic amines (e.g. serotonin, epinephrine, dopamine) and their receptors [23-27] a highly conserved aspartate residue in transmembrane (TM) helix TM3 (Asp 3.32 according to the Ballosteros-Weinstein nomenclature) [28], conserved serine residues in TM5 (e.g. 

Wang CD, Gallaher TK, Shih JC. Site-directed mutagenesis of the serotonin 5-hydroxytrypamine2 receptor identification of amino acids necessary for ligand binding and receptor activation. Mol Pharmacol 1993 43 931-940. 

Manivet P, Schneider B, Smith JC, Choi DS, Maroteaux L, Kellermann O. The serotonin binding site of human and murine 5-HT2B receptors molecular modeling and site-directed mutagenesis. J Biol Chem 2002 277 17,170-17,178. 

Metcalf MA, McGuffin RW, Hamblin MW. Conversion of the human 5-HT1Dp serotonin receptor to the rat 5-HTm ligand-binding phenotype by Thr355Asn site directed mutagenesis. Biochem Pharmacol 1992 44 1917-1920. 

Kao, H.-T., Adham, N., Olsen, M.A., Weinshank, R.L., Branchek, T.A. and Hartig, P.R. (1992) Site-directed mutagenesis of a single residue changes the binding properties of the serotonin 5-HT2 receptor from a human to a rat pharmacology. FEBS Lett. 307 324-328. 

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