Evidence map›Paper›PMID 42115346›Full record

ArticleNature structural & molecular biology2026

Structural basis of PTH1R-β-arrestin core engagement reveals design principles for G-protein-biased therapeutics.

Li-Hua Zhao, Qian He, Qingning Yuan, Min Zhang, Guan-Guan Zhao, Jie Sun, Wen Hu, Hong Shan, H Eric Xu

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2026. 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
–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

1 citing paper in PubMed.

  1. Article
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.

Li-Hua Zhao *Research Center for Medicinal Structural Biology, National Research Center for Translational Medicine at Shanghai, State Key Laboratory of Medical Genomics, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. zlh13131@rjh.com.cn.ORCID http://orcid.org/0000-0002-7175-5174
Qian He *State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Qingning Yuan *Research Center for Medicinal Structural Biology, National Research Center for Translational Medicine at Shanghai, State Key Laboratory of Medical Genomics, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Min ZhangState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Guan-Guan ZhaoState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Jie SunCascade Pharmaceuticals, Pudong District, Shanghai, China.
Wen HuState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Hong ShanState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
H Eric XuResearch Center for Medicinal Structural Biology, National Research Center for Translational Medicine at Shanghai, State Key Laboratory of Medical Genomics, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. eric.xu@simm.ac.cn.ORCID http://orcid.org/0000-0002-6829-8144

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) transmit cellular signals through both G protein and arrestin pathways and biased signaling offers potential therapeutic advantages through selective activation. Although GPCR-G protein complexes are well characterized, structural understanding of class B GPCR-arrestin interactions remains limited. Here we show the cryo-electron microscopy structure of parathyroid hormone receptor 1 in core engagement with β-arrestin 1, revealing the molecular basis of arrestin coupling. The structure shows a rearrangement in which inward movement of extracellular transmembrane helix 5 (TM5) and extracellular loop 3 (ECL3) drives outward displacement of cytoplasmic TM5, forming a configuration required for arrestin binding. Guided by comparison with the G

Indexed as

beta-Arrestin 1beta-ArrestinsGTP-Binding ProteinsReceptor, Parathyroid Hormone, Type 1AnimalsCryoelectron MicroscopyDrug DesignFemaleHumansMiceModels, MolecularProtein BindingProtein Conformationbeta-Arrestin 1beta-ArrestinsGTP-Binding ProteinsPTH1R protein, humanReceptor, Parathyroid Hormone, Type 1

Identifiers

PMID42115346

What Socratic holds

Textmetadata
Read underepoch 390

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 Socratic graph.