Evidence map›Paper›PMID 21575572›Full record

ArticleBiophysical journal2011

A multipoint hydrogen-bond network underlying KcsA C-type inactivation.

Julio F Cordero-Morales, Vishwanath Jogini, Sudha Chakrapani, Eduardo Perozo

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
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

71 citing papers in PubMed, 104 citations in OpenAlex.

  1. Similarity of the ion occupations of KChannels (Austin, Tex.) · 2026
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  10. Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Preparation of GiantBio-protocol · 2021
    Article
  12. Structures of Gating Intermediates in a KJournal of molecular biology · 2021
    Article
  13. Article
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  15. Regulation of KMembranes · 2021
    Article
  16. Article
  17. Article
  18. Exploring KFrontiers in molecular biosciences · 2021
    Article
  19. Article
  20. Article

11 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 at 2 institutions in 1 country.

Julio F Cordero-MoralesDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Vishwanath Jogini
Sudha Chakrapani
Eduardo Perozo
University of Chicago · USD. E. Shaw Research · US

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 GM057846NIGMS NIH HHS R01 GM057846
6 · The paper itself

Abstract

In the prokaryotic potassium channel KcsA activation gating at the inner bundle gate is followed by C-type inactivation at the selectivity filter. Entry into the C-type inactivated state has been directly linked to the strength of the H-bond interaction between residues Glu-71 and Asp-80 behind the filter, and is allosterically triggered by the rearrangement of the inner bundle gate. Here, we show that H-bond pairing between residues Trp-67 and Asp-80, conserved in most K⁺ channels, constitutes another critical interaction that determines the rate and extent of KcsA C-type inactivation. Disruption of the equivalent interaction in Shaker (Trp-434-Asp-447) and Kv1.2 (Trp-366-Asp-379) leads also to modulation of the inactivation process, suggesting that these residues also play an analogous role in the inactivation gating of Kv channels. The present results show that in KcsA C-type inactivation gating is governed by a multipoint hydrogen-bond network formed by the triad Trp-67-Glu71-Asp-80. This triad exerts a critical role in the dynamics and conformational stability of the selectivity filter and might serve as a general modulator of selectivity filter gating in other members of the K⁺ channel family.

Indexed as

Ion Channel GatingAmino Acid SequenceAmino Acid SubstitutionAnimalsAspartic AcidBacterial ProteinsHydrogen BondingModels, MolecularMolecular Sequence DataMutant ProteinsPotassium ChannelsProtein BindingRatsTryptophanXenopusAspartic AcidBacterial ProteinsMutant ProteinsPotassium Channelsprokaryotic potassium channelTryptophan

Identifiers

PMID21575572
PMCPMC3093550
OpenAlexW2070755371

What OpenQuestion holds

Textmetadata
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.