Evidence map›Paper›PMID 31925409›Full record

ArticleNature structural & molecular biology2020

Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture.

Ananth Prasad Burada, Rajesh Vinnakota, Janesh Kumar

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular basis for ligand-gating of the human GluD1 receptor.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Glutamate Delta 1 Receptor in Synapses, Circuits, and Disease.The European journal of neuroscience · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Loss of activation by GABA in vertebrate delta ionotropic glutamate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
    Article
  20. 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

3 authors at 1 institution in 1 country.

Ananth Prasad BuradaLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Pune, Maharashtra, India.ORCID http://orcid.org/0000-0001-9784-1778
Rajesh VinnakotaLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Pune, Maharashtra, India.
Janesh KumarLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Pune, Maharashtra, India. janesh@nccs.res.in.ORCID http://orcid.org/0000-0003-0767-3788
National Centre for Cell Science · IN

Funding

DBT-Wellcome Trust India Alliance IA/I/13/2/501023
6 · The paper itself

Abstract

Ionotropic orphan delta (GluD) receptors are not gated by glutamate or any other endogenous ligand but are grouped with ionotropic glutamate receptors (iGluRs) based on sequence similarity. GluD1 receptors play critical roles in synaptogenesis and synapse maintenance and have been implicated in neuronal disorders, including schizophrenia, cognitive deficits, and cerebral ataxia. Here we report cryo-EM structures of the rat GluD1 receptor complexed with calcium and the ligand 7-chlorokynurenic acid (7-CKA), elucidating molecular architecture and principles of receptor assembly. The structures reveal a non-swapped architecture at the interface of the extracellular amino-terminal domain (ATD) and the ligand-binding domain (LBD). This finding is in contrast with structures of other families of iGluRs, where the dimer partners between the ATD and LBD layers are swapped. Our results demonstrate that principles of architecture and symmetry are not conserved between delta receptors and other iGluRs and provide a molecular blueprint for understanding the functions of the 'orphan' class of iGluRs.

Indexed as

Protein MultimerizationAnimalsCalciumCryoelectron MicroscopyHEK293 CellsHumansKynurenic AcidModels, MolecularProtein ConformationProtein DomainsRatsReceptors, Ionotropic Glutamate7-chlorokynurenic acidCalciumGrid1 protein, ratKynurenic AcidReceptors, Ionotropic Glutamate

Identifiers

PMID31925409
PMCPMC7025878
OpenAlexW3000521212

What OpenQuestion holds

Textmetadata
LicenceTDM
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.