ArticleProceedings of the National Academy of Sciences of the United States of America2009
Probing the role of the cation-pi interaction in the binding sites of GPCRs using unnatural amino acids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The Cation-π Interaction in Chemistry and Biology.Chemical reviews · 2025Review
- A general strategy towards activatable nanophotosensitizer for phototoxicity-free photodynamic therapy.Theranostics · 2025Article
- Deconstructing the transmembrane core of class A G protein-coupled receptors.Trends in biochemical sciences · 2021Review
- Dopamine DInternational journal of molecular sciences · 2021Article
- Emerging strategies for expanding the toolbox of enzymes in biocatalysis.Current opinion in chemical biology · 2020Review
- Dynamic structural rearrangements and functional regulation of voltage-sensing phosphatase.The Journal of physiology · 2019Review
- Progressive fuzzy cation-π assembly of biological catecholamines.Science advances · 2018Article
- Cation-π interactions in protein-ligand binding: theory and data-mining reveal different roles for lysine and arginine.Chemical science · 2018Article
- Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.Accounts of chemical research · 2017Article
- Protein-Observed Fluorine NMR Is a Complementary Ligand Discovery Method toACS chemical biology · 2016Article
- Parametrization of halogen bonds in the CHARMM general force field: Improved treatment of ligand-protein interactions.Bioorganic & medicinal chemistry · 2016Article
- In vivo incorporation of non-canonical amino acids by using the chemical aminoacylation strategy: a broadly applicable mechanistic tool.Chembiochem : a European journal of chemical biology · 2014Review
- Glucose recognition proteins for glucose sensing at physiological concentrations and temperatures.ACS chemical biology · 2014Article
- Ion enrichment on the hydrophobic carbon-based surface in aqueous salt solutions due to cation-π interactions.Scientific reports · 2013Article
- Functionally important aromatic-aromatic and sulfur-π interactions in the D2 dopamine receptor.Journal of the American Chemical Society · 2012Article
- Expression and characterization of the bacterial mechanosensitive channel MscS in Xenopus laevis oocytes.The Journal of general physiology · 2011Article
- Effect of metal Ions (Ni²⁺, Cu²⁺ and Zn²⁺) and water coordination on the structure of L-phenylalanine, L-tyrosine, L-tryptophan and their zwitterionic forms.Journal of molecular modeling · 2011Article
- Dissecting the functions of conserved prolines within transmembrane helices of the D2 dopamine receptor.ACS chemical biology · 2011Article
- Two neuronal nicotinic acetylcholine receptors, alpha4beta4 and alpha7, show differential agonist binding modes.The Journal of biological chemistry · 2011Article
- Third extracellular loop (EC3)-N terminus interaction is important for seven-transmembrane domain receptor function: implications for an activation microswitch region.The Journal of biological chemistry · 2010Article
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Authors and funding
4 authors.
Funding
Abstract
We describe a general application of the nonsense suppression methodology for unnatural amino acid incorporation to probe drug-receptor interactions in functional G protein-coupled receptors (GPCRs), evaluating the binding sites of both the M2 muscarinic acetylcholine receptor and the D2 dopamine receptor. Receptors were expressed in Xenopus oocytes, and activation of a G protein-coupled, inward-rectifying K(+) channel (GIRK) provided, after optimization of conditions, a quantitative readout of receptor function. A number of aromatic amino acids thought to be near the agonist-binding site were evaluated. Incorporation of a series of fluorinated tryptophan derivatives at W6.48 of the D2 receptor establishes a cation-pi interaction between the agonist dopamine and W6.48, suggesting a reorientation of W6.48 on agonist binding, consistent with proposed "rotamer switch" models. Interestingly, no comparable cation-pi interaction was found at the aligning residue in the M2 receptor.
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