Evidence map›Paper›PMID 24051986›Full record

ArticleNature communications2013

Role of the C-terminal domain in the structure and function of tetrameric sodium channels.

Claire Bagnéris, Paul G Decaen, Benjamin A Hall, Claire E Naylor, David E Clapham, Christopher W M Kay, B A Wallace

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.6field-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

52 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. Article
  3. Ion channel selectivity through ion-modulated changes of selectivity filter pProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Light-Activated Assembly of Connexon Nanopores in Synthetic Cells.Journal of the American Chemical Society · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018
    Review
  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

7 authors at 6 institutions in 2 countries.

Claire Bagnéris1] School of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK [2].
Paul G Decaen
Benjamin A Hall
Claire E Naylor
David E Clapham
Christopher W M Kay
B A Wallace
Birkbeck, University of London · GBHarvard University · USHoward Hughes Medical Institute · USInstitute of Structural and Molecular Biology · GBLondon Centre for Nanotechnology · GBMicrosoft Research (United Kingdom) · GB

Funding

SYNAPTIC MECHANISMS IN HIPPOCAMPAL EPILEPTOGENESISP30HD018655 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI POMEROY, SCOTT LOREN · 1985 to 2015
$26.2M
TRP Channel Mediated Pain CircuitryP01NS072040 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI WOOLF, CLIFFORD J · 2011 to 2015
$6.7M
Biotechnology and Biological Sciences Research Council BB/H01070X/1NICHD NIH HHS P30 HD018655NINDS NIH HHS P01 NS072040
6 · The paper itself

Abstract

Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle. A 2.9 Å resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.

Indexed as

Molecular Dynamics SimulationAlphaproteobacteriaAmino Acid SequenceBacterial ProteinsCrystallography, X-RayElectron Spin Resonance SpectroscopyEscherichia coliIon Channel GatingMolecular Sequence DataProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsStatic ElectricityVoltage-Gated Sodium ChannelsBacterial ProteinsRecombinant ProteinsVoltage-Gated Sodium Channels

Identifiers

PMID24051986
PMCPMC3791462
OpenAlexW2161962584

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.