ArticleProceedings of the National Academy of Sciences of the United States of America2017
Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 90 citations in OpenAlex.
- Targeting sweet taste receptor T1R2/T1R3: a new strategy for metabolic disease regulation and intervention of multiple organ diseases.Food chemistry. Molecular sciences · 2026Review
- Free-Space-Coupled Frequency-Locked Microtoroid Resonators with Reactive Polymer Functionalization for Part-Per-Trillion Gas Detection.Laser & photonics reviews · 2026Article
- Molecular mechanism of aspartame recognition by the human sweet taste receptor T1R2-T1R3 revealed by homology modeling and molecular dynamics simulations.Journal of computer-aided molecular design · 2026Article
- Development of a cell-based sweet perception model to study the metabolic effect of different sweeteners.Scientific reports · 2026Article
- Molecular Dynamics Insights into TAS1R2 Transmembrane Domain Activation.International journal of molecular sciences · 2025Article
- Structure-Property Relevance of Two Pairs of Isomeric Steviol Rebaudiosides and the Underlying Mechanism.Foods (Basel, Switzerland) · 2025Article
- Article
- Sweet-enhancing effect of coolant agent menthol evaluated via sensory analysis and molecular modeling.Food chemistry: X · 2025Article
- Ectopic taste receptors in animal physiology: evolutionary conservation and functional diversification.Frontiers in cell and developmental biology · 2025Review
- Steviol rebaudiosides bind to four different sites of the human sweet taste receptor (T1R2/T1R3) complex explaining confusing experiments.Communications chemistry · 2024Article
- Ligand-Dependent and G Protein-Dependent Properties for the Sweet Taste Heterodimer, TAS1R2/1R3.The journal of physical chemistry. B · 2024Article
- Delineating the stepwise millisecond allosteric activation mechanism of the class C GPCR dimer mGlu5.Nature communications · 2024Article
- Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides.Nature communications · 2024Article
- Tongue-on-a-Chip: Parallel Recording of Sweet and Bitter Receptor Responses to Sequential Injections of Pure and Mixed Sweeteners.Journal of agricultural and food chemistry · 2024Article
- Methotrexate Inhibits the Binding of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Receptor Binding Domain to the Host-Cell Angiotensin-Converting Enzyme-2 (ACE-2) Receptor.ACS pharmacology & translational science · 2024Article
- A receptor-based assay to study the sweet and bitter tastes of sweeteners and binary sweet blends: the SWEET project.Chemical senses · 2024Article
- Early-life influences of low-calorie sweetener consumption on sugar taste.Physiology & behavior · 2023Review
- Prediction of dynamic allostery for the transmembrane domain of the sweet taste receptor subunit, TAS1R3.Communications biology · 2023Article
- Scoping Review and Evidence Map of the Relation between Exposure to Dietary Sweetness and Body Weight-Related Outcomes in Adults.Advances in nutrition (Bethesda, Md.) · 2022Article
- The neural basis of sugar preference.Nature reviews. Neuroscience · 2022Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sweet taste in humans is mediated by the TAS1R2/TAS1R3 G protein-coupled receptor (GPCR), which belongs to the class C family that also includes the metabotropic glutamate and γ-aminobutyric acid receptors. We report here the predicted 3D structure of the full-length TAS1R2/TAS1R3 heterodimer, including the Venus Flytrap Domains (VFDs) [in the closed-open (co) active conformation], the cysteine-rich domains (CRDs), and the transmembrane domains (TMDs) at the TM56/TM56 interface. We observe that binding of agonists to VFD2 of TAS1R2 leads to major conformational changes to form a TM6/TM6 interface between TMDs of TAS1R2 and TAS1R3, which is consistent with the activation process observed biophysically on the metabotropic glutamate receptor 2 homodimer. We find that the initial effect of the agonist is to pull the bottom part of VFD3/TAS1R3 toward the bottom part of VFD2/TAS1R2 by ∼6 Å and that these changes get transmitted from VFD2 of TAS1R2 (where agonists bind) through the VFD3 and the CRD3 to the TMD3 of TAS1R3 (which couples to the G protein). These structural transformations provide a detailed atomistic mechanism for the activation process in GPCR, providing insights and structural details that can now be validated through mutation experiments.
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