Abstract
With the help of molecular modelling and computational chemistry a number of residues are identified in the 5HT2and 5-HT1Dreceptor protein sequences as being important for the binding of serotonin. In the 5-HT2receptor the following residues are involved: Trp151Asp155and Phe158in transmcmbranc domain 3 (TM-3), Ser239and Phe240,243,244in TM-5. In the 5-HT,,, receptor: Trp114Asp118and Cys121in TM-3, Thr202 Cys203phe206and Tyr207in TM-5. The obtained models revealed a new concept, the so-called “aromatic box,” which is formed by aromatic residues that constitute the walls and parcel up serotonin. In this box a Cys residue can be the substitute for Phe. For the 5-HT2receptor it is also shown that Asn92Asp120Ser372Asn376and Tyr380can glue TM-1, 2, and7together by a network of hydrogen bonds. Apart form Ser372these residues are conserved among neurotransmitter receptors and are proposed to be important for the receptor architecture.
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© 1993 Springer Science+Business Media Dordrecht
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Janssen, P.A.J., Moereels, H. (1993). Serotonergic Receptors: from Ligands to Sequence. In: Vanhoutte, P.M., Saxena, P.R., Paoletti, R., Brunello, N., Jackson, A.S. (eds) Serotonin. Medical Science Symposia Series, vol 5. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-1920-7_13
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DOI: https://doi.org/10.1007/978-94-011-1920-7_13
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