ArticleBiophysical journal2005
The transmembrane domain of the acetylcholine receptor: insights from simulations on synthetic peptide models.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The central cholinergic system as a therapeutic target in Parkinson's disease.Journal of Parkinson's disease · 2026Review
- Computational design of single-stranded DNA hairpin aptamers immobilized on a biosensor substrate.Scientific reports · 2021Article
- Solid-state NMR (31)P paramagnetic relaxation enhancement membrane protein immersion depth measurements.The journal of physical chemistry. B · 2014Article
- GABA binding to an insect GABA receptor: a molecular dynamics and mutagenesis study.Biophysical journal · 2012Article
- Time-resolved EPR immersion depth studies of a transmembrane peptide incorporated into bicelles.Biochimica et biophysica acta · 2012Article
- Structural characterization of two pore-forming peptides: consequences of introducing a C-terminal tryptophan.Proteins · 2010Article
- Behavioral differences between phosphatidic acid and phosphatidylcholine in the presence of the nicotinic acetylcholine receptor.Biophysical journal · 2008Article
- Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008Review
- Nanosecond-timescale conformational dynamics of the human alpha7 nicotinic acetylcholine receptor.Biophysical journal · 2007Article
- Partitioning of anesthetics into a lipid bilayer and their interaction with membrane-bound peptide bundles.Biophysical journal · 2006Article
- Targeted molecular dynamics study of C-loop closure and channel gating in nicotinic receptors.PLoS computational biology · 2006Article
- An energy-efficient gating mechanism in the acetylcholine receptor channel suggested by molecular and Brownian dynamics.Biophysical journal · 2006Article
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2 authors.
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Abstract
We have studied the structure and properties of a bundle of alpha-helical peptides embedded in a 1,2-dimyristoyl-3-phosphatidylcholine phospholipid bilayer by molecular dynamics simulations. The bundle of five transmembrane deltaM2 segments constitutes the model for the pore region of the nicotinic acetylcholine receptor, which is the neurotransmitter-gated ion-channel responsible for the fast propagation of electrical signals between cells at the nerve-muscle synapse. The deltaM2 segments were shown to oligomerize in biomembranes resulting in ion-channel activity with characteristics similar to the native protein, and the structure of the isolated peptides was studied in 1,2-dimyristoyl-3-phosphatidylcholine bilayers and micelles by NMR experiments (Opella, S. J., et al. 1999. Nat. Struct. Biol. 6:374-379). Our analyses indicate that the structure, helix tilt, and the overall shape of the channel are in good agreement with the NMR experiments and the proposed model for the channel, which we show is formed by rings of functional residues. The studied geometry resulted in a closed pore state, where the channel is partially dehydrated at the hydrophobic extracellular half and the extracellular mouth of the channel blocked by the hydrocarbon chains of Arg+ residues. The arginine amino acids form intermolecular salt-bridges with the C-terminus, which contribute as well to the bundle stabilization.
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