Search results for "umami receptor"
showing 3 items of 3 documents
Characterization of the ligands for the human umami taste receptor
2017
National audience; Among our basics senses, taste and our gustatory system allow us to perceive and recognize essential chemical nutrients present in food. Human can detect and discriminate five basics taste (sweet, bitter, sour, salty and umami) and recent studies proposed a sixth taste for fat. The umami taste is described as a « savory » sensation elicited mainly by L-amino acids and is thought to serve as an indicator of protein rich foods and promote feeding.The umami taste receptor is a heterodimeric receptor composed of the T1R1 and T1R3 subunits. These subunits belong to the family class C G protein-coupled receptors (GPCRs) and are constituted by a large N-terminal domain (NTD) lin…
Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor
2012
Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); 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 characteriza…
An efficient Escherichia coli expression system for the production of a functional N-terminal domain of the T1R3 taste receptor.
2012
http://www.landesbioscience.com/; International audience; 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 …