ArticleBiophysical journal2006
An energy-efficient gating mechanism in the acetylcholine receptor channel suggested by molecular and Brownian dynamics.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Lipid-mediated hydrophobic gating in the BK potassium channel.Nature communications · 2025Article
- Ion transport in muscle acetylcholine receptor maintained by conserved salt bridges between the pore and lipid membrane.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Central cavity dehydration as a gating mechanism of potassium channels.Nature communications · 2023Article
- Article
- Molecular Simulations of Hydrophobic Gating of Pentameric Ligand Gated Ion Channels: Insights into Water and Ions.The journal of physical chemistry. B · 2021Article
- Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3.Sub-cellular biochemistry · 2021Review
- Electric Field Induced Wetting of a Hydrophobic Gate in a Model Nanopore Based on the 5-HTACS nano · 2020Article
- Hydrophobic Gating of Ion Permeation in Magnesium Channel CorA.PLoS computational biology · 2015Article
- Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes.Quarterly reviews of biophysics · 2013Review
- GABA binding to an insect GABA receptor: a molecular dynamics and mutagenesis study.Biophysical journal · 2012Article
- Gating movement of acetylcholine receptor caught by plunge-freezing.Journal of molecular biology · 2012Article
- Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel.Biochimica et biophysica acta · 2012Article
- Functional relationships between agonist binding sites and coupling regions of homomeric Cys-loop receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Testing the applicability of Nernst-Planck theory in ion channels: comparisons with Brownian dynamics simulations.PloS one · 2011Article
- An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation.The Journal of general physiology · 2010Article
- One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Chemical reviews · 2010Review
- An iris-like mechanism of pore dilation in the CorA magnesium transport system.Biophysical journal · 2010Article
- Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues.The Journal of physiology · 2010Review
- Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors.The Journal of physiology · 2010Review
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1 author.
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Abstract
Acetylcholine receptors mediate electrical signaling between nerve and muscle by opening and closing a transmembrane ion conductive pore. Molecular and Brownian dynamics simulations are used to shed light on the location and mechanism of the channel gate. Four separate 5 ns molecular dynamics simulations are carried out on the imaged structure of the channel, a hypothetical open structure with a slightly wider pore and a mutant structure in which a central ring of hydrophobic residues is replaced by polar groups. Water is found to partially evacuate the pore during molecular simulations of the imaged structure, whereas ions face a large energy barrier and do not conduct through the channel in Brownian dynamics simulations. The pore appears to be in a closed configuration despite containing an unobstructed pathway across the membrane as a series of hydrophobic residues in the center of the channel provide an unfavorable home to water and ions. When the channel is widened slightly, water floods into the channel and ions conduct at a rate comparable to the currents measured experimentally in open channels. The pore remains permeable to ions provided the extracellular end of the pore-lining helix is restrained near the putative open configuration to mimic the presence of the ligand binding domain. Replacing some of the hydrophobic residues with polar ones decreases the barrier for ion permeation but does not result in significant currents. The channel is posited to utilize an energy efficient gating mechanism in which only minor conformational changes of the hydrophobic region of the pore are required to create macroscopic changes in conductance.
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