ArticleBiophysical journal2009
Energy and structure of the M2 helix in acetylcholine receptor-channel gating.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Computational discovery of natural inhibitors targeting enterovirus D68 3C protease using molecular docking pharmacokinetics and dynamics simulations.Scientific reports · 2025Article
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
- Article
- Agonist efficiency from concentration-response curves: Structural implications and applications.Biophysical journal · 2021Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- Mutations Causing Slow-Channel Myasthenia Reveal That a Valine Ring in the Channel Pore of Muscle AChR is Optimized for Stabilizing Channel Gating.Human mutation · 2016Article
- Heterologous expression and nonsense suppression provide insights into agonist behavior at α6β2 nicotinic acetylcholine receptors.Neuropharmacology · 2015Article
- Function of the M1 π-helix in endplate receptor activation and desensitization.The Journal of physiology · 2015Article
- Molecular interactions between mecamylamine enantiomers and the transmembrane domain of the human α4β2 nicotinic receptor.Biochemistry · 2014Article
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Loop C and the mechanism of acetylcholine receptor-channel gating.The Journal of general physiology · 2013Article
- Structural basis for ion permeation mechanism in pentameric ligand-gated ion channels.The EMBO journal · 2013Article
- Energy for wild-type acetylcholine receptor channel gating from different choline derivatives.Biophysical journal · 2013Article
- Action of nicotine and analogs on acetylcholine receptors having mutations of transmitter-binding site residue αG153.The Journal of general physiology · 2013Article
- Energetic contributions to channel gating of residues in the muscle nicotinic receptor β1 subunit.PloS one · 2013Article
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Drying transition in the hydrophobic gate of the GLIC channel blocks ion conduction.Biophysical journal · 2012Article
- An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors.The Journal of general physiology · 2012Article
- The energetic consequences of loop 9 gating motions in acetylcholine receptor-channels.The Journal of physiology · 2012Article
- Linear rate-equilibrium relations arising from ion channel-bilayer energetic coupling.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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3 authors.
Funding
Abstract
We studied single-channel currents from neuromuscular acetylcholine receptor-channels with mutations in the pore-lining, M2 helix of the epsilon-subunit. Three parameters were quantified: 1), the diliganded gating equilibrium constant (E(2)), which reflects the energy difference between C(losed) and O(pen) conformations; 2), the correlation between the opening rate constant and E(2) on a log-log scale (Phi), which illuminates the energy character of the residue (C- versus O-like) within the C<-->O isomerization process; and 3), the open-channel current amplitude (i(0)), which reports whether a mutation alters the energetics of ion permeation. The largest E(2) changes were observed in the cytoplasmic half of epsilonM2 (5', 9', 12', 13', and 16'), with smaller changes apparent for residues > or =17'. Phi was approximately 0.54 for most epsilonM2 residues, but was approximately 0.32 at the positions that had largest E(2) changes. An arginine substitution reduced i(0) significantly at six positions, with the magnitude of the reduction increasing, 16'-->2'. The measurements suggest that the 9', 12', and 13' residues experience large and late free-energy changes in the channel-opening process. We speculate that in the gating isomerization the pore-facing residues >6' and <16' experience multiple energy perturbations associated with changes in protein structure and, perhaps, hydration.
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