Evidence map›Paper›PMID 21170050›Full record

ArticleNature structural & molecular biology2011

Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.

David T Wang, Adam P Hill, Stefan A Mann, Peter S Tan, Jamie I Vandenberg

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Modulation of hERG KFrontiers in pharmacology · 2020
    Review
  9. An Update on the Structure of hERG.Frontiers in pharmacology · 2019
    Review
  10. Ether-à-go-go KThe Journal of physiology · 2018
    Review
  11. Towards a Structural View of Drug Binding to hERG KTrends in pharmacological sciences · 2017
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015
    Review
  19. Article
  20. Getting to the heart of hERG K(+) channel gating.The Journal of physiology · 2015
    Review
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

5 authors.

David T WangMark Cowley Lidwill Research Program in Cardiac Electrophysiology, Molecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, New South Wales, Australia. j.vandenberg@victorchang.edu.au
Adam P Hill
Stefan A Mann
Peter S Tan
Jamie I Vandenberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The potassium channel selectivity filter both discriminates between K(+) and sodium ions and contributes to gating of ion flow. Static structures of conducting (open) and nonconducting (inactivated) conformations of this filter are known; however, the sequence of protein rearrangements that connect these two states is not. We show that closure of the selectivity filter gate in the human K(v)11.1 K(+) channel (also known as hERG, for ether-a-go-go-related gene), a key regulator of the rhythm of the heartbeat, is initiated by K(+) exit, followed in sequence by conformational rearrangements of the pore domain outer helix, extracellular turret region, voltage sensor domain, intracellular domains and pore domain inner helix. In contrast to the simple wave-like sequence of events proposed for opening of ligand-gated ion channels, a complex spatial and temporal sequence of widespread domain motions connect the open and inactivated states of the K(v)11.1 K(+) channel.

Indexed as

ERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsHumansIon Channel GatingKineticsPotassiumProtein Structure, TertiaryERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsKCNH2 protein, humanPotassium

Identifiers

PMID21170050

What OpenQuestion holds

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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.