ArticleProtein expression and purification2012
Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor.
Article in Protein expression and purification, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 44 citations in OpenAlex.
- Artificial sweeteners stimulate adipogenesis and suppress lipolysis independently of sweet taste receptors.The Journal of biological chemistry · 2013Trial
- Sweet and umami TAS1R receptors: from molecular recognition to physiological function.Chemical senses · 2026Review
- Glutathione as a taste modulator: molecular mechanisms of interaction with umami and sweet taste receptors.Food chemistry. Molecular sciences · 2025Article
- Inosine-5'-monophosphate interacts with the TAS1R3 subunit to enhance sweet taste detection.Food chemistry. Molecular sciences · 2025Article
- Steviol rebaudiosides bind to four different sites of the human sweet taste receptor (T1R2/T1R3) complex explaining confusing experiments.Communications chemistry · 2024Article
- A receptor-based assay to study the sweet and bitter tastes of sweeteners and binary sweet blends: the SWEET project.Chemical senses · 2024Article
- Functional Characterization of the Venus Flytrap Domain of the Human TAS1R2 Sweet Taste Receptor.International journal of molecular sciences · 2022Article
- Pharmacology of TAS1R2/TAS1R3 Receptors and Sweet Taste.Handbook of experimental pharmacology · 2022Article
- Biophysical and functional characterization of the human TAS1R2 sweet taste receptor overexpressed in a HEK293S inducible cell line.Scientific reports · 2021Article
- Structure-Function Analyses of Human Bitter Taste Receptors-Where Do We Stand?Molecules (Basel, Switzerland) · 2020Review
- Allelic variation of the Tas1r3 taste receptor gene affects sweet taste responsiveness and metabolism of glucose in F1 mouse hybrids.PloS one · 2020Article
- Novel Site-Specific Fatty Chain-Modified GLP-1 Receptor Agonist with Potent Antidiabetic Effects.Molecules (Basel, Switzerland) · 2019Article
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- Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate Their Species-Specific Sweetness Tasting Properties.Molecules (Basel, Switzerland) · 2018Article
- Structure-Function Relationships of Olfactory and Taste Receptors.Chemical senses · 2018Review
- A large-scale expression strategy for multimeric extracellular protein complexes using Drosophila S2 cells and its application to the recombinant expression of heterodimeric ligand-binding domains of taste receptor.Protein science : a publication of the Protein Society · 2017Article
- Potential inhibitors designed against NDM-1 type metallo-β-lactamases: an attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteria.Scientific reports · 2017Article
- Structural basis for perception of diverse chemical substances by T1r taste receptors.Nature communications · 2017Article
- Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characterization, we overexpressed the human NTD of T1R3 (hT1R3-NTD) using Escherichia coli in the form of inclusion bodies. Using a fractional factorial screen coupled to a functional assay, conditions were determined for the refolding of hT1R3-NTD. Far-UV circular dichroism spectroscopic studies revealed that hT1R3-NTD was well refolded. Using size-exclusion chromatography, we found that the refolded protein behaves as a dimer. Ligand binding quantified by tryptophan fluorescence quenching and microcalorimetry showed that hT1R3-NTD is functional and capable of binding sucralose with an affinity in the millimolar range. This study also provides a strategy to produce functional hT1R3-NTD by heterologous expression in E. coli; this is a prerequisite for structural determination and functional analysis of ligand-binding regions of other class C GPCRs.
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