Evidence map›Paper›PMID 27150040›Full record

ArticleStructure (London, England : 1993)2016

Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.

Kimberly Matulef, Alvin W Annen, Jay C Nix, Francis I Valiyaveetil

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Structures of Gating Intermediates in a KJournal of molecular biology · 2021
    Article
  9. Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. High-Resolution Structures of KHandbook of experimental pharmacology · 2021
    Article
  14. Article
  15. TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  16. Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020
    Review
  17. Review
  18. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  19. Article
  20. 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

4 authors.

Kimberly MatulefProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health & Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA.
Alvin W AnnenProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health & Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA.
Jay C NixMolecular Biology Consortium, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Francis I ValiyaveetilProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health & Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA. Electronic address: valiyave@ohsu.edu.

Funding

Probing functional mechanisms in K+ channels using unnatural mutagenesisR01GM087546 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI VALIYAVEETIL, FRANCIS · 2009 to 2022
$4.0M
NIGMS NIH HHS R01 GM087546
6 · The paper itself

Abstract

The selectivity filter of K(+) channels contains four ion binding sites (S1-S4) and serves dual functions of discriminating K(+) from Na(+) and acting as a gate during C-type inactivation. C-type inactivation is modulated by ion binding to the selectivity filter sites, but the underlying mechanism is not known. Here we evaluate how the ion binding sites in the selectivity filter of the KcsA channel participate in C-type inactivation and in recovery from inactivation. We use unnatural amide-to-ester substitutions in the protein backbone to manipulate the S1-S3 sites and a side-chain substitution to perturb the S4 site. We develop an improved semisynthetic approach for generating these amide-to-ester substitutions in the selectivity filter. Our combined electrophysiological and X-ray crystallographic analysis of the selectivity filter mutants show that the ion binding sites play specific roles during inactivation and provide insights into the structural changes at the selectivity filter during C-type inactivation.

Indexed as

Bacterial ProteinsBinding SitesIon Channel GatingMutationPotassiumPotassium ChannelsProtein BindingBacterial ProteinsPotassiumPotassium Channelsprokaryotic potassium channel

Identifiers

PMID27150040
PMCPMC4876015

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.