ArticleBioengineered
An efficient Escherichia coli expression system for the production of a functional N-terminal domain of the T1R3 taste receptor.
Article in Bioengineered. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Inosine-5'-monophosphate interacts with the TAS1R3 subunit to enhance sweet taste detection.Food chemistry. Molecular sciences · 2025Article
- Functional Characterization of the Venus Flytrap Domain of the Human TAS1R2 Sweet Taste Receptor.International journal of molecular sciences · 2022Article
- Biophysical and functional characterization of the human TAS1R2 sweet taste receptor overexpressed in a HEK293S inducible cell line.Scientific reports · 2021Article
- Current Progress in Understanding the Structure and Function of Sweet Taste Receptor.Journal of molecular neuroscience : MN · 2021Review
- Article
- A self-inducible heterologous protein expression system in Escherichia coli.Scientific reports · 2016Article
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4 authors at 2 institutions in 1 country.
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Abstract
Sweet taste is mediated by a dimeric receptor composed of two distinct subunits, T1R2 and T1R3, whereas the T1R1/T1R3 receptor is involved in umami taste perception. The T1R1, T1R2, and T1R3 subunits are members of the small family of class C G protein-coupled receptors (GPCRs). The members of this family are characterized by a large N-terminal domain (NTD), which is structurally similar to bacterial periplasmic-binding proteins and contains the primary ligand-binding site. In a recent study, we described a strategy to produce a functional dimeric human T1R3-NTD. Although the protein was expressed as inclusion bodies (IBs) using the Escherichia coli system, the conditions for the refolding of functional hT1R3-NTD were determined using a fractional factorial screen coupled to a binding assay. Here, we report that this refolding strategy can be used to produce T1R1- and T1R2-NTDs in large quantities. We also discuss that our findings could be more generally applicable to other class C GPCR-NTDs, including the γ-aminobutyric acid type B receptor (GABABR), the extracellular calcium-sensing receptor (CaSR) and the large family of pheromone (V2R) orphan receptors.
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