Evidence map›Paper›PMID 31308429›Full record

ArticleScientific reports2019

Atomistic mechanisms underlying the activation of the G protein-coupled sweet receptor heterodimer by sugar alcohol recognition.

Panupong Mahalapbutr, Nitchakan Darai, Wanwisa Panman, Aunchan Opasmahakul, Nawee Kungwan, Supot Hannongbua, Thanyada Rungrotmongkol

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
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

18 citing papers in PubMed, 40 citations in OpenAlex.

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  14. Frontiers in immunology · 2021
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  17. Structural insight into the recognition ofComputational and structural biotechnology journal · 2020
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Panupong MahalapbutrStructural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Nitchakan DaraiProgram in Biotechnology, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Wanwisa PanmanMultidisciplinary Program of Petrochemistry and Polymer Science, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Aunchan OpasmahakulComputational Chemistry Center of Excellent, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Nawee KungwanDepartment of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand.
Supot HannongbuaComputational Chemistry Center of Excellent, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Thanyada RungrotmongkolStructural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand. t.rungrotmongkol@gmail.com.
Chulalongkorn University · THChiang Mai University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human T1R2-T1R3 sweet taste receptor (STR) plays an important role in recognizing various low-molecular-weight sweet-tasting sugars and proteins, resulting in the release of intracellular heterotrimeric G protein that in turn leads to the sweet taste perception. Xylitol and sorbitol, which are naturally occurring sugar alcohols (polyols) found in many fruits and vegetables, exhibit the potential caries-reducing effect and are widely used for diabetic patients as low-calorie sweeteners. In the present study, computational tools were applied to investigate the structural details of binary complexes formed between these two polyols and the T1R2-T1R3 heterodimeric STR. Principal component analysis revealed that the Venus flytrap domain (VFD) of T1R2 monomer was adapted by the induced-fit mechanism to accommodate the focused polyols, in which α-helical residues 233-268 moved significantly closer to stabilize ligands. This finding likely suggested that these structural transformations might be the important mechanisms underlying polyols-STR recognitions. The calculated free energies also supported the VFD of T1R2 monomer as the preferential binding site for such polyols, rather than T1R3 region, in accord with the lower number of accessible water molecules in the T1R2 pocket. The E302 amino acid residue in T1R2 was found to be the important recognition residue for polyols binding through a strongly formed hydrogen bond. Additionally, the binding affinity of xylitol toward the T1R2 monomer was significantly higher than that of sorbitol, making it a sweeter tasting molecule.

Indexed as

Binding SitesCell MembraneDimerizationHumansLigandsModels, MolecularReceptors, G-Protein-CoupledSorbitolSugar AlcoholsSweetening AgentsTasteTaste PerceptionXylitolLigandsReceptors, G-Protein-CoupledSorbitolSugar AlcoholsSweetening Agentstaste receptors, type 1Xylitol

Identifiers

PMID31308429
PMCPMC6629994
OpenAlexW2959804098

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

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.