Evidence map›Paper›PMID 22678295›Full record

ArticleNature2012

Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel.

Xu Zhang, Wenlin Ren, Paul DeCaen, Chuangye Yan, Xiao Tao, Lin Tang, Jingjing Wang, Kazuya Hasegawa, Takashi Kumasaka, Jianhua He and 3 more

Abstract read
In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 269 papers.

0numbers the graph read from it
0cells of the map it votes in
269citing papers in PubMed
23.6field-weighted citation impact, top 1% 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

269 citing papers in PubMed, 477 citations in OpenAlex.

  1. Suzetrigine, a NaMolecules (Basel, Switzerland) · 2026
    Review
  2. HInternational journal of molecular sciences · 2025
    Review
  3. Review
  4. Article
  5. Voltage sensors.Molecular pharmacology · 2025
    Review
  6. Article
  7. A structural atlas of druggable sites on NaChannels (Austin, Tex.) · 2024
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Voltage sensors of a NaNature communications · 2023
    Article
  15. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  16. 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
  17. Cannabidiol inhibits NaNature communications · 2023
    Article
  18. Structural mapping of NaNature communications · 2023
    Article
  19. Article
  20. Article

209 more citing papers are in PubMed but not listed here.

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

13 authors at 8 institutions in 3 countries.

Xu ZhangState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, Tsinghua University, Beijing 100084, China.
Wenlin Ren
Paul DeCaen
Chuangye Yan
Xiao Tao
Lin Tang
Jingjing Wang
Kazuya Hasegawa
Takashi Kumasaka
Jianhua He
Jiawei Wang
David E Clapham
Nieng Yan
Tsinghua University · CNCenter for Life Sciences · CNHoward Hughes Medical Institute · USShanghai Institute of Applied Physics · CNChinese Academy of Sciences · CNHarvard University · USJapan Synchrotron Radiation Research Institute · JPSPring-8 · JP

Funding

RESEARCH METHODS IN PEDIATRICS HEART DISEASET32HL007572 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI Sarah D DE FERRANTI, Jane W. Newburger · 1985 to 2026
$13.0M
TRP Channel Mediated Pain CircuitryP01NS072040 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI WOOLF, CLIFFORD J · 2011 to 2015
$6.7M
Howard Hughes Medical InstituteNHLBI NIH HHS T32 HL007572NINDS NIH HHS P01 NS072040
6 · The paper itself

Abstract

Voltage-gated sodium (Na(v)) channels are essential for the rapid depolarization of nerve and muscle, and are important drug targets. Determination of the structures of Na(v) channels will shed light on ion channel mechanisms and facilitate potential clinical applications. A family of bacterial Na(v) channels, exemplified by the Na(+)-selective channel of bacteria (NaChBac), provides a useful model system for structure-function analysis. Here we report the crystal structure of Na(v)Rh, a NaChBac orthologue from the marine alphaproteobacterium HIMB114 (Rickettsiales sp. HIMB114; denoted Rh), at 3.05 Å resolution. The channel comprises an asymmetric tetramer. The carbonyl oxygen atoms of Thr 178 and Leu 179 constitute an inner site within the selectivity filter where a hydrated Ca(2+) resides in the crystal structure. The outer mouth of the Na(+) selectivity filter, defined by Ser 181 and Glu 183, is closed, as is the activation gate at the intracellular side of the pore. The voltage sensors adopt a depolarized conformation in which all the gating charges are exposed to the extracellular environment. We propose that Na(v)Rh is in an 'inactivated' conformation. Comparison of Na(v)Rh with Na(v)Ab reveals considerable conformational rearrangements that may underlie the electromechanical coupling mechanism of voltage-gated channels.

Indexed as

Ion Channel GatingAlphaproteobacteriaAmino Acid SequenceBacterial ProteinsCrystallizationCrystallography, X-RayHEK293 CellsHumansModels, MolecularMolecular Sequence DataProtein ConformationSodium ChannelsStructure-Activity RelationshipBacterial ProteinsNaChBac protein, bacteriaSodium Channels

Identifiers

PMID22678295
PMCPMC3979295
OpenAlexW2054058473

What OpenQuestion holds

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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.