Evidence map›Paper›PMID 39945513›Full record

ArticleeLife2025

CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting.

Yangyu Wu, Yangyang Yan, Youshan Yang, Shumin Bian, Alberto Rivetta, Ken Allen, Fred J Sigworth

Abstract read
In one paragraph

Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. LaIT6: A Novel Insect-Selective KMolecules (Basel, Switzerland) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Electric field-induced pore constriction in the human KProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Harnessing AlphaFold to reveal hERG channel conformational state secrets.bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Plural molecular and cellular mechanisms of pore domainbioRxiv : the preprint server for biology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Yangyu WuDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.ORCID https://orcid.org/0000-0001-8064-6132
Yangyang YanDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.
Youshan YangDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.
Shumin BianDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.
Alberto RivettaDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.
Ken AllenDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.
Fred J SigworthDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, United States.ORCID https://orcid.org/0000-0002-7178-8494

Funding

FLUCTUATIONS IN IONIC CURRENT THROUGH MEMBRANE CHANNELSR01NS021501 · NINDS · YALE UNIVERSITY · PI SIGWORTH, FREDERICK J · 1985 to 2024
$10.9M
High-throughput electron cryo-microscopeS10OD023603 · OD · YALE UNIVERSITY · PI SIGWORTH, FREDERICK J · 2018 to 2018
$1.9M
NIH HHS R01NS021501NIH HHS S10 OD023603NIH HHS S10OD023603NINDS NIH HHS R01 NS021501
6 · The paper itself

Abstract

We present near-atomic-resolution cryoEM structures of the mammalian voltage-gated potassium channel Kv1.2 in open, C-type inactivated, toxin-blocked and sodium-bound states at 3.2 Å, 2.5 Å, 3.2 Å, and 2.9 Å. These structures, all obtained at nominally zero membrane potential in detergent micelles, reveal distinct ion-occupancy patterns in the selectivity filter. The first two structures are very similar to those reported in the related Shaker channel and the much-studied Kv1.2-2.1 chimeric channel. On the other hand, two new structures show unexpected patterns of ion occupancy. First, the toxin α-Dendrotoxin, like Charybdotoxin, is seen to attach to the negatively-charged channel outer mouth, and a lysine residue penetrates into the selectivity filter, with the terminal amine coordinated by carbonyls, partially disrupting the outermost ion-binding site. In the remainder of the filter two densities of bound ions are observed, rather than three as observed with other toxin-blocked Kv channels. Second, a structure of Kv1.2 in Na

Indexed as

Kv1.2 Potassium ChannelAnimalsCryoelectron MicroscopyModels, MolecularProtein ConformationSodiumKv1.2 Potassium ChannelSodiumbiophysicscryoEMdendrotoxininactivationion selectivitymolecular biophysicsneuroscienceratstructural biologyvoltage sensor

Identifiers

PMID39945513
PMCPMC11825129

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.