Evidence map›Paper›PMID 20153331›Full record

ArticleFEBS letters2010

Design and characterization of a constitutively open KcsA.

Luis G Cuello, Vishwanath Jogini, D Marien Cortes, Amornrat Sompornpisut, Michael D Purdy, Michael C Wiener, Eduardo Perozo

Abstract read
In one paragraph

Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Ion-binding properties of a K+ channel selectivity filter in different conformations.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Article
  11. Article
  12. Importance of lipid-pore loop interface for potassium channel structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Article
  14. Article
  15. Mechanism of activation gating in the full-length KcsA K+ channel.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. 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

7 authors.

Luis G CuelloDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Vishwanath Jogini
D Marien Cortes
Amornrat Sompornpisut
Michael D Purdy
Michael C Wiener
Eduardo Perozo

Funding

HIGH RESOLUTION STRUCTURAL DYNAMICS OF K CHANNELSR01GM057846 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PEROZO, EDUARDO A · 1998 to 2018
$7.4M
NIGMS NIH HHS R01 GM057846NIGMS NIH HHS R01-GM57846
6 · The paper itself

Abstract

The molecular nature of the structure responsible for proton sensitivity in KcsA has been identified as a charge cluster that surrounds the inner helical bundle gate. Here, we show that this proton sensor can be modified to engineer a constitutively open form of KcsA, amenable to functional, spectroscopic and structural analyses. By combining charge neutralizations for all acidic and basic residues in the cluster at positions 25, 117-122 and 124 (but not E118), a mutant KcsA is generated that displays constitutively open channel activity up to pH 9. The structure of this mutant revealed that full opening appears to be inhibited by lattice forces since the activation gate seems to be only on the early stages of opening.

Indexed as

Amino Acid SequenceBacterial ProteinsCloning, MolecularCrystallography, X-RayIon Channel GatingModels, MolecularMutant ProteinsPotassium ChannelsProtein ConformationProtein EngineeringStructural Homology, ProteinBacterial ProteinsMutant ProteinsPotassium Channelsprokaryotic potassium channel

Identifiers

PMID20153331
PMCPMC2848999

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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.