Evidence map›Paper›PMID 30455434›Full record

ArticleNature structural & molecular biology2018

High-resolution crystal structure of parathyroid hormone 1 receptor in complex with a peptide agonist.

Janosch Ehrenmann, Jendrik Schöppe, Christoph Klenk, Mathieu Rappas, Lutz Kummer, Andrew S Doré, Andreas Plückthun

Abstract read
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Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing 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

72 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. A novel brachydactyly type E syndrome caused by variants in helix 8 of the PTH1R.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2026
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  14. The function of GPCRs in different bone cells.International journal of biological sciences · 2025
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  20. Article

12 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Janosch Ehrenmann *Department of Biochemistry, University of Zürich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4447-9298
Jendrik Schöppe *Department of Biochemistry, University of Zürich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-2689-5549
Christoph Klenk *Department of Biochemistry, University of Zürich, Zurich, Switzerland. c.klenk@bioc.uzh.ch.ORCID http://orcid.org/0000-0001-5199-7144
Mathieu RappasSosei Heptares, Granta Park, Cambridge, UK.
Lutz KummerDepartment of Biochemistry, University of Zürich, Zurich, Switzerland.
Andrew S DoréSosei Heptares, Granta Park, Cambridge, UK.
Andreas PlückthunDepartment of Biochemistry, University of Zürich, Zurich, Switzerland. plueckthun@bioc.uzh.ch.ORCID http://orcid.org/0000-0003-4191-5306
University of Zurich · CHHeptares Therapeutics (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parathyroid hormone 1 receptor (PTH1R) is a class B multidomain G-protein-coupled receptor (GPCR) that controls calcium homeostasis. Two endogenous peptide ligands, parathyroid hormone (PTH) and parathyroid hormone-related protein (PTHrP), activate the receptor, and their analogs teriparatide and abaloparatide are used in the clinic to increase bone formation as an effective yet costly treatment for osteoporosis. Activation of PTH1R involves binding of the peptide ligand to the receptor extracellular domain (ECD) and transmembrane domain (TMD), a hallmark of class B GPCRs. Here, we present the crystal structure of human PTH1R in complex with a peptide agonist at 2.5-Å resolution, allowing us to delineate the agonist binding mode for this receptor and revealing molecular details within conserved structural motifs that are critical for class B receptor function. Thus, this study provides structural insight into the function of PTH1R and extends our understanding of this therapeutically important class of GPCRs.

Indexed as

Amino Acid SequenceBiomimeticsCrystallography, X-RayHumansModels, MolecularParathyroid HormonePeptidesProtein BindingReceptor, Parathyroid Hormone, Type 1Parathyroid HormonePeptidesPTH1R protein, humanReceptor, Parathyroid Hormone, Type 1

Identifiers

PMID30455434
OpenAlexW2899995053

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.