Evidence map›Paper›PMID 11969415›Full record

ArticleBiochemistry2002

Structure of the transition state of gating in the acetylcholine receptor channel pore: a phi-value analysis.

Gisela D Cymes, Claudio Grosman, Anthony Auerbach

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. Article
  9. The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

3 authors.

Gisela D CymesCenter for Single-Molecule Biophysics and Department of Physiology and Biophysics, State University of New York at Buffalo, Buffalo, New York 14214, USA.
Claudio Grosman
Anthony Auerbach

Funding

MULTIPLE ACTIVITY PATTERNS OF ACETYLCHOLINE RECEPTORSR37NS023513 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI AUERBACH, ANTHONY L · 2000 to 2013
$6.9M
Mechanisms of Neurotransmitter-Gated Ion ChannelsR01NS042169 · NINDS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GROSMAN, CLAUDIO F · 2003 to 2022
$6.6M
Multiple Activity Patterns of Acetylcholine ReceptorsR56NS023513 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI AUERBACH, ANTHONY L · 2014 to 2014
$530k
MULTIPLE ACTIVITY PATTERNS OF ACETYLCHOLINE RECEPTORSR01NS023513 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI AUERBACH, ANTHONY L · 1987 to 1999
–
NCRR NIH HHS RR11111NINDS NIH HHS NS23513NINDS NIH HHS R01 NS023513NINDS NIH HHS R37 NS023513NINDS NIH HHS R56 NS023513
6 · The paper itself

Abstract

The gating mechanism of the acetylcholine receptor channel (AChR) was investigated by using rate equilibrium linear free energy relationships (LFERs) to probe the transition state between the closed and open conformations. The properties of the transition state of gating in the second transmembrane segment (M2) of the delta subunit, one of the five homologous pore-lining segments, was measured on a residue-by-residue basis. Series of point mutations were engineered at individual positions of this domain, and the corresponding constructs were characterized electrophysiologically, at the single-channel level. Fully liganded AChR opening and closing rate constants were estimated, and Phi-values (which are a measure of the extent of the conformational change realized at the transition state) were calculated for each reaction series as the slope of the Brønsted relationship (log rate constant versus log equilibrium constant). Our results indicate that, at the transition state of gating, the extracellular half of deltaM2 partly resembles the open state (Phi-values between 0.24 and 0.38) while the intracellular half completely resembles the closed state (Phi-values between -0.18 and 0.03), with a break point near the middle of the M2 segment. This suggests that during gating the two halves of deltaM2 move asynchronously, with the rearrangement of the extracellular portion preceding (following) that of the intracellular part of deltaM2 during opening (closing). This particular sequence of molecular events indicates that the gating conformational change, which starts at the extracellular acetylcholine-binding sites (when opening), does not propagate exclusively along the primary sequence of the protein. In addition, our data are consistent with the deltaM2 segment bending or swiveling around its central residues during gating. We also elaborate on unsettled aspects of the analysis such as the accuracy of two-point LFERs, the physical interpretation of fractional Phi-values, and the existence of single versus parallel transition states for the gating reaction.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsCell LineExtracellular SpaceHumansIntracellular FluidLinear Energy TransferMiceModels, ChemicalMolecular Sequence DataMuscle, SkeletalMutagenesis, Site-DirectedPatch-Clamp TechniquesPeptide FragmentsPeptidesM2 deltaPeptide FragmentsPeptidesReceptor, Muscarinic M2Receptors, Muscarinic

Identifiers

PMID11969415
PMCPMC6442467

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.