ArticleBiophysical journal2005
Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.
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 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses.Pharmacological research · 2015Review
- Molecular dynamics simulation of the antiamoebin ion channel: linking structure and conductance.Biophysical journal · 2011Article
- Soft wall ion channel in continuum representation with application to modeling ion currents in α-hemolysin.The journal of physical chemistry. B · 2010Article
- 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
- Calcium inhibits paracellular sodium conductance through claudin-2 by competitive binding.The Journal of biological chemistry · 2010Article
- Structural characterization of two pore-forming peptides: consequences of introducing a C-terminal tryptophan.Proteins · 2010Article
- Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site.The Journal of general physiology · 2009Article
- Anion-cation permeability correlates with hydrated counterion size in glycine receptor channels.Biophysical journal · 2008Article
- In silico models for the human alpha4beta2 nicotinic acetylcholine receptor.The journal of physical chemistry. B · 2008Article
- Computational prediction of ion permeation characteristics in the glycine receptor modified by photo-sensitive compounds.Journal of computer-aided molecular design · 2008Article
- Diffusion constant of K+ inside Gramicidin A: a comparative study of four computational methods.Biophysical chemistry · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The pentameric glycine receptor (GlyR), a member of the nicotinicoid superfamily of ligand-gated ion channels, is an inhibitory Cl(-) channel that is gated by glycine. Using recently published NMR data of the second transmembrane segment (M2) of the human alpha1 GlyR, structural models of pentameric assemblies embedded in a lipid bilayer were constructed using a combination of experimentally determined constraints coupled with all-atom energy minimization. Based on this structure of the pentameric M2 "pore", Brownian dynamics simulations of ion permeation through this putative conducting open state of the channel were carried out. Simulated I-V curves were in good agreement with published experimental current-voltage curves and the anion/cation permeability ratio, suggesting that our open-state model may be representative of the conducting channel of the full-length receptor. These studies also predicted regions of chloride occupancy and suggested residues critical to anion permeation. Calculations of the conductance of the cation-selective mutant A251E channel are also consistent with experimental data. In addition, both rotation and untilting of the pore helices of our model were found to be broadly consistent with closing of the channel, albeit at distinct regions that may reflect alternate gates of the receptor.
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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.