Evidence map›Paper›PMID 31753620›Full record

ArticleStructure (London, England : 1993)2020

A Refined Open State of the Glycine Receptor Obtained via Molecular Dynamics Simulations.

Marc A Dämgen, Philip C Biggin

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Human GlyRα2 pore dynamics in gating and inhibition.Structure (London, England : 1993) · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Dynamics and Interplay of the Binding Pockets in the Glycine Receptor.Journal of chemical information and modeling · 2025
    Article
  8. Article
  9. Article
  10. Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. When is a hydrophobic gate not a hydrophobic gate?The Journal of general physiology · 2022
    Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Marc A DämgenStructural Bioinformatics and Computational Biochemistry, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Philip C BigginStructural Bioinformatics and Computational Biochemistry, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: philip.biggin@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S001247/1
6 · The paper itself

Abstract

Pentameric ligand-gated ion channels are key players in mediating fast neurotransmission. Glycine receptors are chloride-selective members of this receptor family that mediate inhibitory synaptic transmission and are implicated in neurological disorders including autism and hyperekplexia. They have been structurally characterized by both X-ray crystallography and cryoelectron microscopy (cryo-EM) studies, with the latter giving rise to what was proposed as a possible open state. However, recent work has questioned the physiological relevance of this open state structure, since it rapidly collapses in molecular dynamics simulations. Here, we show that the collapse can be avoided by a careful equilibration protocol that reconciles the more problematic regions of the original density map and gives a stable open state that shows frequent selective chloride permeation. The protocol developed in this work provides a means to refine open-like structures of the whole pentameric ligand-gated ion channel superfamily and reconciles the previous issues with the cryo-EM structure.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsLeucineModels, MolecularMolecular Dynamics SimulationProtein ConformationProtein MultimerizationReceptors, GlycineLeucineReceptors, Glycinecomputationalcryo-EMCys-loop receptorsligand-gated ion channelsmembrane structurepermeationrefinementselectivitysimulation

Identifiers

PMID31753620
PMCPMC6945115
OpenAlexW2985182034

What OpenQuestion holds

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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.