Evidence map›Paper›PMID 33027636›Full record

ArticleStructure (London, England : 1993)2021

Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.

Shanti Pal Gangwar, Marriah N Green, Erwan Michard, Alexander A Simon, José A Feijó, Alexander I Sobolevsky

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.5field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Plants (Basel, Switzerland) · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
    Article
  15. CaThe EMBO journal · 2022
    Review
  16. Article
  17. Review
  18. Review
  19. 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

6 authors at 3 institutions in 1 country.

Shanti Pal GangwarDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA.
Marriah N GreenDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA; Training Program in Nutritional and Metabolic Biology, Institute of Human Nutrition, Columbia University Irving Medical Center, 630 West 168(th) Street, New York, NY 10032, USA.
Erwan MichardDepartment of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA.
Alexander A SimonDepartment of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA.
José A FeijóDepartment of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA. Electronic address: jfeijo@umd.edu.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA. Electronic address: as4005@cumc.columbia.edu.
University of Maryland, College Park · USColumbia University Irving Medical Center · USColumbia University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
NUTRITIONT32DK007647 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI Anthony W Ferrante, Lori M Zeltser · 1990 to 2026
$7.4M
Structure and Function of AMPA subtype ionotropic glutamate receptorsR01NS083660 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KURNIKOVA, MARIA G, SOBOLEVSKY, ALEXANDER · 2013 to 2022
$4.3M
Structure and function of Transient Receptor Potential ChannelsR01CA206573 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2017 to 2026
$3.8M
Single-Particle Cryo-EM Characterization of AMPA Receptor Functional StatesR01NS107253 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2018 to 2026
$3.5M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
The role of Cornichon Homologue proteins in cytosolic calcium homeostasis through sorting and activity of plant ionotropic- Glutamate Receptor-Like channelsR01GM131043 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI FEIJO, JOSE A · 2019 to 2022
$1.4M
NCI NIH HHS R01 CA206573NCRR NIH HHS S10 RR029205NIDDK NIH HHS T32 DK007647NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM131043NINDS NIH HHS R01 NS083660NINDS NIH HHS R01 NS107253
6 · The paper itself

Abstract

Glutamate receptor-like channels (GLRs) play important roles in numerous plant physiological processes. GLRs are homologous to ionotropic glutamate receptors (iGluRs) that mediate neurotransmission in vertebrates. Here we determine crystal structures of Arabidopsis thaliana GLR3.2 ligand-binding domain (LBD) in complex with glycine and methionine to 1.58- and 1.75-Å resolution, respectively. Our structures show a fold similar to that of iGluRs, but with several secondary structure elements either missing or different. The closed clamshell conformation of GLR3.2 LBD suggests that both glycine and methionine act as agonists. The mutation R133A strongly increases the constitutive activity of the channel, suggesting that the LBD mutated at the residue critical for agonist binding produces a more stable closed clamshell conformation. Furthermore, our structures explain the promiscuity of GLR activation by different amino acids, confirm evolutionary conservation of structure between GLRs and iGluRs, and predict common molecular principles of their gating mechanisms driven by bilobed clamshell-like LBDs.

Indexed as

ArabidopsisArabidopsis ProteinsBinding SitesIon Channel GatingMolecular Dynamics SimulationProtein BindingReceptors, GlutamateArabidopsis ProteinsGLR3.2 protein, ArabidopsisReceptors, GlutamateCa(2+) channelsglutamate receptor-like channels (GLR)ionotropic glutamate receptor (iGluR)plantX-ray crystallography

Identifiers

PMID33027636
PMCPMC7867599
OpenAlexW3092077924

What OpenQuestion holds

Textmetadata
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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.