Sweet taste receptor (TAS1R2-TAS1R3 heterodimer) (TAS1R2-TAS1R3)

The **sweet taste receptor** is a heterodimer composed of two subunits, **TAS1R2** and **TAS1R3**, both members of the class C G protein-coupled receptor (GPCR) family[2][3][1][5][6]. The obligate heterodimer is localized to taste cells in the tongue and is responsible for sensing a wide range of sweet compounds, including natural sugars, artificial sweeteners, and sweet-tasting proteins[2][3][1][6]. Each subunit contains a Venus flytrap domain, a cysteine-rich domain, and a seven-transmembrane domain; the functional receptor requires both subunits, with sweet ligand binding occurring primarily at the Venus flytrap domain of TAS1R2[2][3][7][1][5]. Activation of the receptor leads to GPCR-mediated intracellular signaling via gustducin and other pathways, driving the perception of sweetness[4][2]. Beyond taste, it may also participate in metabolic regulation, linking dietary choices to metabolic health. Although it is not a classic drug target, the sweet taste receptor is significant for food science, obesity research, and potentially for the design of new therapeutics or nutritional interventions targeting metabolic diseases via modulation of taste and sugar perception[2][3].

Other names

Sweet taste receptor heterodimerType 1 taste receptor heterodimerTAS1R2-TAS1R3 receptorT1R2-T1R3 receptor

Agonism (activation of the receptor by binding to the Venus flytrap domain, primarily on TAS1R2, leading to conformational changes and initiating downstream GPCR signaling)[2][3][7][1]. Allosteric modulation (proposed binding sites for various modulators influencing receptor activity)[1]