Evidence map›Paper›PMID 34815401›Full record

ArticleNature communications2021

Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5.

Eunyoung Jeong, Yoojoong Kim, Jihong Jeong, Yunje Cho

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Article
  6. Article
  7. Osteocalcin and GPR158: linking bone and brain function.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Constitutive activation mechanism of a class C GPCR.Nature structural & molecular biology · 2024
    Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Eunyoung Jeong *Department of Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea.ORCID http://orcid.org/0000-0002-5872-4330
Yoojoong Kim *Department of Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea.ORCID http://orcid.org/0000-0003-2881-6856
Jihong JeongDepartment of Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea.ORCID http://orcid.org/0000-0002-5567-4753
Yunje ChoDepartment of Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea. yunje@postech.ac.kr.ORCID http://orcid.org/0000-0001-6481-1716
Pohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Gαi/o protein signaling through the RGS7-Gβ5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gβ5 heterodimers. GPR158 dimerizes through Per-Arnt-Sim-fold extracellular and transmembrane (TM) domains connected by an epidermal growth factor-like linker. The TM domain (TMD) reflects both inactive and active states of other class C GPCRs: a compact intracellular TMD, conformations of the two intracellular loops (ICLs) and the TMD interface formed by TM4/5. The ICL2, ICL3, TM3, and first helix of the cytoplasmic coiled-coil provide a platform for the DHEX domain of one RGS7 and the second helix recruits another RGS7. The unique features of the RGS7-binding site underlie the selectivity of GPR158 for RGS7.

Indexed as

Cryoelectron MicroscopyGTP-Binding Protein beta SubunitsHEK293 CellsHumansReceptors, G-Protein-CoupledRecombinant ProteinsRGS ProteinsGNB5 protein, humanGPR158 protein, humanGTP-Binding Protein beta SubunitsReceptors, G-Protein-CoupledRecombinant ProteinsRGS7 protein, humanRGS Proteins

Identifiers

PMID34815401
PMCPMC8611064
OpenAlexW3216763196

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.