ArticleMolecular pharmacology2011
A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists.
Article in Molecular pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hidden Interactions: Quantum Perspectives in Drug Design.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Article
- Genetic Code Expansion for Mechanistic Studies in Ion Channels: An (Un)natural Union of Chemistry and Biology.Chemical reviews · 2024Review
- Probing the functional hotspots inside protein hydrophobic pockets byChemical science · 2024Article
- Expression and purification of fluorinated proteins from mammalian suspension culture.Methods in enzymology · 2024Article
- Article
- Multiple regions in the extracellular domain of the glycine receptor determine receptor activity.The Journal of biological chemistry · 2018Article
- The roles of aromatic residues in the glycine receptor transmembrane domain.BMC neuroscience · 2018Article
- Probing the molecular basis of hERG drug block with unnatural amino acids.Scientific reports · 2018Article
- Functional Consequences of the Postnatal Switch From Neonatal to Mutant Adult Glycine Receptor α1 Subunits in theFrontiers in molecular neuroscience · 2018Article
- A systematic analysis of atomic protein-ligand interactions in the PDB.MedChemComm · 2017Article
- The GlyR Extracellular β8-β9 Loop - A Functional Determinant of Agonist Potency.Frontiers in molecular neuroscience · 2017Article
- Structure and Pharmacologic Modulation of Inhibitory Glycine Receptors.Molecular pharmacology · 2016Review
- Genetic and functional analyses demonstrate a role for abnormal glycinergic signaling in autism.Molecular psychiatry · 2016Article
- Cation-π interactions: computational analyses of the aromatic box motif and the fluorination strategy for experimental evaluation.Physical chemistry chemical physics : PCCP · 2015Article
- A molecular characterization of the agonist binding site of a nematode cys-loop GABA receptor.British journal of pharmacology · 2015Article
- Disturbed neuronal ER-Golgi sorting of unassembled glycine receptors suggests altered subcellular processing is a cause of human hyperekplexia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Incorporation of Non-Canonical Amino Acids.Advances in experimental medicine and biology · 2015Review
- Disturbances of Ligand Potency and Enhanced Degradation of the Human Glycine Receptor at Affected Positions G160 and T162 Originally Identified in Patients Suffering from Hyperekplexia.Frontiers in molecular neuroscience · 2015Article
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7 authors.
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Abstract
Cation-π interactions have been demonstrated to play a major role in agonist-binding in Cys-loop receptors. However, neither the aromatic amino acid contributing to this interaction nor its location is conserved among Cys-loop receptors. Likewise, it is not clear how many different agonists of a given receptor form a cation-π interaction or, if they do, whether it is with the same aromatic amino acid as the major physiological agonist. We demonstrated previously that Phe159 in the glycine receptor (GlyR) α1 subunit forms a strong cation-π interaction with the principal agonist, glycine. In the current study, we investigated whether the lower efficacy agonists of the human GlyR β-alanine and taurine also form cation-π interactions with Phe159. By incorporating a series of unnatural amino acids, we found cation-π interactions between Phe159 and the amino groups of β-alanine and taurine. The strengths of these interactions were significantly weaker than for glycine. Modeling studies suggest that β-alanine and taurine are orientated subtly differently in the binding pocket, with their amino groups further from Phe159 than that of glycine. These data therefore show that similar agonists can have similar but not identical orientations and interactions in the binding pocket and provide a possible explanation for the lower potencies of β-alanine and taurine.
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