Selective polypeptide ligand binding to the extracellular surface of the transmembrane domains of the class B GPCRs GLP-1R and GCGR.

Huixia Wang, Wanhui Hu, Tiandan Xu, Ya Yuan, Dongsheng Liu, Kurt Wüthrich

Open access · goldAbstract read

In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.8field-weighted citation impact, top 25% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

GPCR Biased Signaling in Metabolism.Handbook of experimental pharmacology · 2026
Review

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

6 authors at 3 institutions in 2 countries.

Huixia WangIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Wanhui HuIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Tiandan XuIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Ya YuanIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Dongsheng LiuIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Kurt WüthrichIHuman Institute, ShanghaiTech University, Shanghai 201210, China.

ShanghaiTech University · CNChinese Academy of Sciences · CNScripps Institution of Oceanography · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crystal and cryo-EM structures of the glucagon-like peptide-1 receptor (GLP-1R) and glucagon receptor (GCGR) bound with their peptide ligands have been obtained with full-length constructs, indicating that the extracellular domain (ECD) is indispensable for specific ligand binding. This article complements these data with studies of ligand recognition of the two receptors in solution. Paramagnetic NMR relaxation enhancement measurements using dual labeling with fluorine-19 probes on the receptor and nitroxide spin labels on the peptide ligands provided new insights. The glucagon-like peptide-1 (GLP-1) was found to interact with GLP-1R by selective binding to the extracellular surface. The ligand selectivity toward the extracellular surface of the receptor was preserved in the transmembrane domain (TMD) devoid of the ECD. The dual labeling approach further provided evidence of cross-reactivity of GLP-1R and GCGR with glucagon and GLP-1, respectively, which is of interest in the context of medical treatments using combinations of the two polypeptides.

Indexed as

Biological sciencesmolecular biologymolecular interactionmolecular structure

Identifiers

PMID37332600

DOI10.1016/j.isci.2023.106918

PMCPMC10276138

OpenAlexW4377115717

What OpenQuestion holds

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LicenceCC BY-NC-ND

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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.