ReviewJournal of molecular neuroscience : MN2010
On the origin of ion selectivity in the Cys-loop receptor family.
Review in Journal of molecular neuroscience : MN, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biophysical characterization of calcium-binding and modulatory-domain dynamics in a pentameric ligand-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- High-resolution structures of multiple 5-HTeLife · 2020Article
- Structural basis for allosteric transitions of a multidomain pentameric ligand-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Cryo-EM structure of 5-HTNature communications · 2018Article
- Chemogenetic Tools for Causal Cellular and Neuronal Biology.Physiological reviews · 2018Review
- Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014Review
- Molecular dissection of Cl--selective Cys-loop receptor points to components that are dispensable or essential for channel activity.The Journal of biological chemistry · 2011Article
- Emerging Pharmacological Properties of Cholinergic Synaptic Transmission: Comparison between Mammalian and Insect Synaptic and Extrasynaptic Nicotinic Receptors.Current neuropharmacology · 2011Article
- Rings of charge within the extracellular vestibule influence ion permeation of the 5-HT3A receptor.The Journal of biological chemistry · 2011Article
- Ion selectivity mechanism in a bacterial pentameric ligand-gated ion channel.Biophysical journal · 2011Article
- Acetylcholine receptor (AChR) α5 subunit variant associated with risk for nicotine dependence and lung cancer reduces (α4β2)₂α5 AChR function.Molecular pharmacology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
Agonist binding to Cys-loop receptors promotes a large transmembrane ion flux of several million cations or anions per second. To investigate structural bases for the dynamics (MD) simulations, X-ray crystallography, and single channel recording. MD simulations of the muscle nicotinic receptor, imbedded in a lipid bilayer with an applied transmembrane potential, reveal single cation translocation events during transient periods of channel hydration. During the simulation trajectory, cations paused for prolonged periods near several rings of anionic residues projecting from the lumen of the extracellular domain of the receptor, but subsequently the cation moved rapidly through the hydrophobic transmembrane region as the constituent alpha-helices exhibited back and forth rocking motions. Cocrystallization of acetylcholine binding protein with sulfate ions revealed coordination of five sulfates with residues from one of these charged rings; in cation-selective Cys-loop receptors this ring contains negatively charged residues, whereas in anion-selective receptors it contains positively charged residues. In the muscle nicotinic receptor, charge reversal of residues of this ring decreases unitary conductance by up to 80%. Thus in Cys-loop receptors, a series of charged rings along the ion translocation pathway concentrates hydrated ions relative to bulk solution, giving rise to charge selectivity, and then subtle motions of the hydrophobic transmembrane, coupled with transient periods of water filling, enable rapid ion flux.
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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.