ArticleBiophysical journal2004
A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Comparative analysis of isoxazoline activity on human and canine GABA receptors expressed in Xenopus oocytes.Parasites & vectors · 2025Article
- Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008Review
- Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.BMC neuroscience · 2008Article
- Functional asymmetry of transmembrane segments in nicotinic acetylcholine receptors.European biophysics journal : EBJ · 2006Article
- Probing ion-channel pores one proton at a time.Nature · 2005Article
- Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.Biophysical journal · 2005Article
- A gating mechanism proposed from a simulation of a human alpha7 nicotinic acetylcholine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: structure and collective motions.Biophysical journal · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nicotinic acetylcholine receptor is a neurotransmitter-gated ion channel in the postsynaptic membrane. It is composed of five homologous subunits, each of which contributes one transmembrane helix--the M2 helix--to create the channel pore. The M2 helix from the delta subunit is capable of forming a channel by itself. Although a model of the receptor was recently proposed based on a low-resolution, cryo-electron microscopy density map, we found that the model does not explain much of the other available experimental data. Here we propose a new model of the M2 channel derived solely from helix packing and symmetry constraints. This model agrees well with experimental results from solid-state NMR, chemical reactivity, and mutagenesis experiments. The model depicts the channel pore, the channel gate, and the residues responsible for cation specificity.
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Registered trials
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.