ArticleProceedings of the National Academy of Sciences of the United States of America2005
Pore conformations and gating mechanism of a Cys-loop receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Key role of the TM2-TM3 loop in calcium potentiation of the α9α10 nicotinic acetylcholine receptor.Cellular and molecular life sciences : CMLS · 2024Article
- The nicotinic acetylcholine receptor: a typical 'allosteric machine'.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Trapping of ivermectin by a pentameric ligand-gated ion channel upon open-to-closed isomerization.Scientific reports · 2017Article
- Allosteric regulation of pentameric ligand-gated ion channels: an emerging mechanistic perspective.Channels (Austin, Tex.) · 2014Review
- Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activation.ACS chemical neuroscience · 2013Article
- Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes.Quarterly reviews of biophysics · 2013Review
- Size matters in activation/inhibition of ligand-gated ion channels.Trends in pharmacological sciences · 2012Review
- Synaptic neurotransmitter-gated receptors.Cold Spring Harbor perspectives in biology · 2012Review
- Molecular mechanisms of Cys-loop ion channel receptor modulation by ivermectin.Frontiers in molecular neuroscience · 2012Article
- 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
- Chloride ions in the pore of glycine and GABA channels shape the time course and voltage dependence of agonist currents.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Ion selectivity mechanism in a bacterial pentameric ligand-gated ion channel.Biophysical journal · 2011Article
- Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model.PLoS computational biology · 2011Article
- Molecular dynamics and brownian dynamics investigation of ion permeation and anesthetic halothane effects on a proton-gated ion channel.Journal of the American Chemical Society · 2010Article
- Structure-function study of the fourth transmembrane segment of the GABAρ1 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Probing pore constriction in a ligand-gated ion channel by trapping a metal ion in the pore upon agonist dissociation.The Journal of biological chemistry · 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
- Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues.The Journal of physiology · 2010Review
- Structural basis of activation of cys-loop receptors: the extracellular-transmembrane interface as a coupling region.Molecular neurobiology · 2009Review
- Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurons regulate the propagation of chemoelectric signals throughout the nervous system by opening and closing ion channels, a process known as gating. Here, histidine-based metal-binding sites were engineered along the intrinsic pore of a chimeric Cys-loop receptor to probe state-dependent Zn(2+)-channel interactions. Patterns of Zn(2+) ion binding within the pore reveal that, in the closed state, the five pore-lining segments adopt an oblique orientation relative to the axis of ion conduction and constrict into a physical gate at their intracellular end. The interactions of Zn(2+) with the open state indicate that the five pore-lining segments should rigidly tilt to enable the movement of their intracellular ends away from the axis of ion conduction, so as to open the constriction (i.e., the gate). Alignment of the functional results with the 3D structure of an acetylcholine receptor allowed us to generate structural models accounting for the closed and open pore conformations and for a gating mechanism of a Cys-loop receptor.
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