Introduction of TAS2R16
Taste receptor type 2 member 16 (TAS2R16) is a protein that in humans is encoded by the TAS2R16 gene, which is located on the long (q) arm of chromosome 7 at position 31.1-31.3, from base pair 122,228,764 to base pair 122,229,639. As a member of the family of taste type 2 receptors (TAS2Rs), TAS2R16 is reported to play a role in the perception of bitterness.
|Basic Information of TAS2R16|
|Protein Name||Taste receptor type 2 member 16|
|Organism||Homo sapiens (Human)|
Function of TAS2R16 Membrane Protein
Human bitter taste perception is mediated by the 25 members of the highly divergent TAS2R receptor family, which are seven transmembranes G protein-coupled receptors that are mainly expressed in specialized taste bud cells. The TAS2Rs are also expressed in the respiratory and gastrointestinal tracts and have evolved to detect the extraordinary diversity of bitter compounds that are naturally found in foods and toxins, translating that detection into gustatory perception via G protein-coupled signaling. As a member of the TAS2R receptor family, TAS2R16 is reported to respond to ~30 different β-glucoside compounds, whose molecular scaffold consists of a D-glucose monosaccharide linked by an oxygen atom to a phenyl group. During the past years, TAS2R16 specifically is believed to play a central role in determining human preference to eat or avoid foods with bitter β-glucosides, important dietary choices that ultimately influence human health.
Fig.1 TAS2R16 residues that define ligand specificity. (Thomas, 2017)
Application of TAS2R16 Membrane Protein in Literature
This article aims to evaluate whether polymorphic variants in TAS2R16 could affect the risk of developing this neoplasia and identify the role of TAS2R16 in modulating chronic inflammation within the gut. It suggests that polymorphisms within TAS2R16 gene do not have a strong influence on colon cancer susceptibility, but a possible role in rectal cancer should be further evaluated in larger cohorts.
This article suggests a model in which hydrophobic residues on TM3 and TM7 form a broad ligand-binding pocket that can accommodate the diverse structural features of β-glycoside ligands while still achieving high specificity.
This report finds that the sensitivity of TAS2R16 varied due to several amino acid residues. Mutation of amino acid residues at E86T, L247M, and V260F in human and langur TAS2R16 for mimicking the macaque TAS2R16 decreased the sensitivity of the receptor in an additive manner, which suggests its contribution to the potency of salicin, possibly via direct interaction.
This article aims to investigate the sensitivities of TAS2R16s of various primates and finds that the sensitivity of each primate species varied according to the ligand. It suggests that the possibility that bitter-taste sensitivities evolved independently by replacing specific amino acid residues of TAS2Rs in different primate species to adapt to food items they use.
This article suggests that there is a correlation between TAS2R16 and the recognition of a specific chemical structure to the perception of bitter taste. If the ability of TAS2R16 to detect substances with common molecular properties is typical of the bitter receptor family, it may explain how a few receptors permit the perception of numerous bitter substances.
TAS2R16 Preparation Options
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