Evidence map›Paper›PMID 20574420›Full record

ArticleNature2010

Structure of the gating ring from the human large-conductance Ca(2+)-gated K(+) channel.

Yunkun Wu, Yi Yang, Sheng Ye, Youxing Jiang

Abstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing 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

130 citing papers in PubMed.

  1. Review
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  7. Andrology · 2025
    Review
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  9. Article
  10. Redox-dependent CdBiophysical journal · 2024
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Mitochondrial potassium channels: A novel calcitriol target.Cellular & molecular biology letters · 2022
    Article
  20. Article

70 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

4 authors.

Yunkun WuDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA.
Yi Yang
Sheng Ye
Youxing Jiang

Funding

Mechanism of Ligand Gating in Potassium ChannelsR01GM071621 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, YOUXING · 2004 to 2008
$1.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM071621
6 · The paper itself

Abstract

Large-conductance Ca(2+)-gated K(+) (BK) channels are essential for many biological processes such as smooth muscle contraction and neurotransmitter release. This group of channels can be activated synergistically by both voltage and intracellular Ca(2+), with the large carboxy-terminal intracellular portion being responsible for Ca(2+) sensing. Here we present the crystal structure of the entire cytoplasmic region of the human BK channel in a Ca(2+)-free state. The structure reveals four intracellular subunits, each comprising two tandem RCK domains, assembled into a gating ring similar to that seen in the MthK channel and probably representing its physiological assembly. Three Ca(2+) binding sites including the Ca(2+) bowl are mapped onto the structure based on mutagenesis data. The Ca(2+) bowl, located within the second RCK domain, forms an EF-hand-like motif and is strategically positioned close to the assembly interface between two subunits. The other two Ca(2+) (or Mg(2+)) binding sites, Asp 367 and Glu 374/Glu 399, are located on the first RCK domain. The Asp 367 site has high Ca(2+) sensitivity and is positioned in the groove between the amino- and carboxy-terminal subdomains of RCK1, whereas the low-affinity Mg(2+)-binding Glu 374/Glu 399 site is positioned on the upper plateau of the gating ring and close to the membrane. Our structure also contains the linker connecting the transmembrane and intracellular domains, allowing us to dock a voltage-gated K(+) channel pore of known structure onto the gating ring with reasonable accuracy and generate a structural model for the full BK channel.

Indexed as

Ion Channel GatingBinding SitesCalciumCrystallography, X-RayCytoplasmHumansLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMagnesiumModels, MolecularProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsCalciumKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMagnesiumProtein Subunits

Identifiers

PMID20574420
PMCPMC2910425

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Registered trials

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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.