Evidence map›Paper›PMID 28798468›Full record

ArticleScientific reports2017

The Bitter Taste Receptor TAS2R16 Achieves High Specificity and Accommodates Diverse Glycoside Ligands by using a Two-faced Binding Pocket.

Anu Thomas, Chidananda Sulli, Edgar Davidson, Eli Berdougo, Morganne Phillips, Bridget A Puffer, Cheryl Paes, Benjamin J Doranz, Joseph B Rucker

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. GengricinInternational journal of molecular sciences · 2024
    Trial
  2. Intracellular and dual-site inhibition of a bitter taste GPCR.Cellular and molecular life sciences : CMLS · 2026
    Article
  3. Article
  4. Bitter taste receptors.Chemical senses · 2025
    Review
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  6. Article
  7. Review
  8. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Anu ThomasIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Chidananda SulliIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Edgar DavidsonIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Eli BerdougoIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Morganne PhillipsIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Bridget A PufferIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Cheryl PaesIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Benjamin J DoranzIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA.
Joseph B RuckerIntegral Molecular, Inc., 3711 Market St, Suite 900, Philadelphia, PA, 19104, USA. jrucker@integralmolecular.com.

Funding

Engineering of membrane protein chemosensors for therapeutic researchR44DC010105 · NIDCD · INTEGRAL MOLECULAR · PI RUCKER, JOSEPH BENJAMIN · 2014 to 2016
$1.2M
Development of taste receptor ligands using structure-activity studiesR43DC010105 · NIDCD · INTEGRAL MOLECULAR · PI RUCKER, JOSEPH BENJAMIN · 2009 to 2010
$696k
NIDCD NIH HHS R43 DC010105NIDCD NIH HHS R44 DC010105
6 · The paper itself

Abstract

Although bitter taste receptors (TAS2Rs) are important for human health, little is known of the determinants of ligand specificity. TAS2Rs such as TAS2R16 help define gustatory perception and dietary preferences that ultimately influence human health and disease. Each TAS2R must accommodate a broad diversity of chemical structures while simultaneously achieving high specificity so that diverse bitter toxins can be detected without all foods tasting bitter. However, how these G protein-coupled receptors achieve this balance is poorly understood. Here we used a comprehensive mutation library of human TAS2R16 to map its interactions with existing and novel agonists. We identified 13 TAS2R16 residues that contribute to ligand specificity and 38 residues whose mutation eliminated signal transduction by all ligands, providing a comprehensive assessment of how this GPCR binds and signals. Our data suggest 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.

Indexed as

Binding SitesGlycosidesHEK293 CellsHumansMolecular Docking SimulationProtein BindingReceptors, G-Protein-CoupledSubstrate SpecificityTaste Receptors, Type 2GlycosidesReceptors, G-Protein-CoupledTaste Receptors, Type 2

Identifiers

PMID28798468
PMCPMC5552880

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.