Evidence map›Paper›PMID 25848005›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.

Yu Zhou, Xiao-Ming Xia, Christopher J Lingle

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Redox-dependent CdBiophysical journal · 2024
    Article
  3. Review
  4. Article
  5. The functionally relevant site for paxilline inhibition of BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. 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

3 authors.

Yu ZhouDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110 zhouy@wustl.edu clingle@morpheus.wustl.edu.
Xiao-Ming XiaDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110.
Christopher J LingleDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110 zhouy@wustl.edu clingle@morpheus.wustl.edu.

Funding

STRUCTURE/ACTIVITY STUDIES OF NEUROSTEROID ANALOGUESP01GM047969 · NIGMS · WASHINGTON UNIVERSITY · PI COVEY, DOUGLAS F · 1992 to 2011
$18.7M
Ion Channel Regulation by Ca2+R01GM066215 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2003 to 2015
$3.6M
NIGMS NIH HHS GM066215NIGMS NIH HHS P01 GM047969NIGMS NIH HHS R01 GM066215
6 · The paper itself

Abstract

To probe structure and gating-associated conformational changes in BK-type potassium (BK) channels, we examined consequences of Cd(2+) coordination with cysteines introduced at two positions in the BK inner pore. At V319C, the equivalent of valine in the conserved Kv proline-valine-proline (PVP) motif, Cd(2+) forms intrasubunit coordination with a native glutamate E321, which would place the side chains of V319C and E321 much closer together than observed in voltage-dependent K(+) (Kv) channel structures, requiring that the proline between V319C and E321 introduces a kink in the BK S6 inner helix sharper than that observed in Kv channel structures. At inner pore position A316C, Cd(2+) binds with modest state dependence, suggesting the absence of an ion permeation gate at the cytosolic side of BK channel. These results highlight fundamental structural differences between BK and Kv channels in their inner pore region, which likely underlie differences in voltage-dependent gating between these channels.

Indexed as

Amino Acid SequenceAnimalsCadmiumCrystallography, X-RayCysteineGlutamic AcidIntracellular SpaceIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsModels, MolecularMolecular Sequence DataMutant ProteinsProtein SubunitsStructure-Activity RelationshipXenopusCadmiumCysteineGlutamic AcidLarge-Conductance Calcium-Activated Potassium ChannelsMutant ProteinsProtein SubunitsBK channelsCd2+ coordinationK+ channelsSlo1 channelsstate dependence

Identifiers

PMID25848005
PMCPMC4413310

What OpenQuestion holds

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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.