Evidence map›Paper›PMID 22579978›Full record

ArticleBiochimica et biophysica acta2012

Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel.

Annika F Barber, Vincenzo Carnevale, S G Raju, Cristiano Amaral, Werner Treptow, Michael L Klein

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The chemical basis for electrical signaling.Nature chemical biology · 2017
    Review
  11. Small molecule modulation of voltage gated sodium channels.Current opinion in structural biology · 2017
    Review
  12. Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Review
  14. Review
  15. Modulation of a voltage-gated Na+ channel by sevoflurane involves multiple sites and distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Article
  18. Exploring conformational states of the bacterial voltage-gated sodium channel NavAb via molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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 2 countries.

Annika F BarberDepartment of Neuroscience and Graduate Program in Cell and Developmental Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Vincenzo Carnevale
S G Raju
Cristiano Amaral
Werner Treptow
Michael L Klein
Temple University · USUniversidade de Brasília · BRThomas Jefferson University · US

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BLASIE, J. KENT · 1997 to 2017
$22.4M
Alcohol Tissue InjuryT32AA007463 · NIAAA · THOMAS JEFFERSON UNIVERSITY · PI HOEK, JOANNES B, VADIGEPALLI, RAJANIKANTH · 1985 to 2021
$9.1M
Molecular interactions of general anesthetics in voltage-gated sodium channelsF31NS077689 · NINDS · THOMAS JEFFERSON UNIVERSITY · PI BARBER, ANNIKA FITZPATRICK · 2011 to 2013
$67k
NIAAA NIH HHS T32 AA007463NIGMS NIH HHS P01 GM055876NINDS NIH HHS F31 NS077689
6 · The paper itself

Abstract

Computational methods and experimental data are used to provide structural models for NaChBac, the homo-tetrameric voltage-gated sodium channel from the bacterium Bacillus halodurans, with a closed and partially open pore domain. Molecular dynamic (MD) simulations on membrane-bound homo-tetrameric NaChBac structures, each comprising six helical transmembrane segments (labeled S1 through S6), reveal that the shape of the lumen, which is defined by the bundle of four alpha-helical S6 segments, is modulated by hinge bending motions around the S6 glycine residues. Mutation of these glycine residues into proline and alanine affects, respectively, the structure and conformational flexibility of the S6 bundle. In the closed channel conformation, a cluster of stacked phenylalanine residues from the four S6 helices hinders diffusion of water molecules and Na(+) ions. Activation of the voltage sensor domains causes destabilization of the aforementioned cluster of phenylalanines, leading to a more open structure. The conformational change involving the phenylalanine cluster promotes a kink in S6, suggesting that channel gating likely results from the combined action of hinge-bending motions of the S6 bundle and concerted reorientation of the aromatic phenylalanine side-chains.

Indexed as

BacillusBacterial ProteinsBiophysicsGlycineIon Channel GatingIonsMembrane PotentialsModels, MolecularMolecular ConformationMolecular Dynamics SimulationMotionPhenylalanineProtein ConformationProtein Structure, SecondaryProtein Structure, TertiarySodiumBacterial ProteinsGlycineIonsPhenylalanineSodiumSodium ChannelsVoltage-Gated Sodium Channels

Identifiers

PMID22579978
PMCPMC3378804
OpenAlexW2111573861

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.