3 results match your criteria tyr143 tyr153

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Exploring the binding of serotonin to the 5-HT3 receptor by density functional theory.

J Phys Chem B 2006 Dec;110(51):26313-9

Physics Department, King's College London, Strand, London WC2R 2LS, United Kingdom.

The 5-HT3 receptor is a typical ligand-gated ion channel of the Cys-loop superfamily, which is activated by binding of serotonin (5-HT). Models of the binding site of this protein reveal potential interactions between 5-HT and Tyr143, Tyr153, and Tyr234. Here we describe a series of ab initio calculations, based on density functional theory, to assess the effects of mutating these tyrosine residues on the binding of 5-HT. Read More

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December 2006

Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis.

J Neurosci 2004 Oct;24(41):9097-104

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.

The mechanism by which agonist binding triggers pore opening in ligand-gated ion channels is poorly understood. Here, we used unnatural amino acid mutagenesis to introduce subtle changes to the side chains of tyrosine residues (Tyr141, Tyr143, Tyr153, and Tyr234), which dominate the 5-HT3 receptor binding site. Heterologous expression in oocytes, combined with radioligand binding data and a model of 5-HT (serotonin) computationally docked into the binding site, has allowed us to determine which of these residues are responsible for binding and/or gating. Read More

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October 2004

The role of tyrosine residues in the extracellular domain of the 5-hydroxytryptamine3 receptor.

J Biol Chem 2004 May 3;279(22):23294-301. Epub 2004 Mar 3.

Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.

Aromatic residues play an important role in the ligand-binding domain of Cys loop receptors. Here we examine the role of the 11 tyrosines in this domain of the 5-HT3 receptor in ligand binding and receptor function by substituting them for alanine, for serine, and, for some residues, also for phenylalanine. The mutant receptors were expressed in HEK293 cells and Xenopus oocytes and examined using radioligand binding, Ca2+ imaging, electrophysiology, and immunochemistry. Read More

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