ArticleThe Journal of general physiology2004
Gating dynamics of the acetylcholine receptor extracellular domain.
Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed.
- A release of local subunit conformational heterogeneity underlies gating in a muscle nicotinic acetylcholine receptor.Nature communications · 2024Article
- αACS chemical neuroscience · 2022Article
- GABAFrontiers in cellular neuroscience · 2020Article
- The effects of insecticides on two splice variants of the glutamate-gated chloride channel receptor of the major malaria vector, Anopheles gambiae.British journal of pharmacology · 2020Article
- Ketamine Inhibition of the Pentameric Ligand-Gated Ion Channel GLIC.Biophysical journal · 2017Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels.PLoS biology · 2016Article
- Agonist activation of a nicotinic acetylcholine receptor.Neuropharmacology · 2015Review
- Putative chanzyme activity of TRPM2 cation channel is unrelated to pore gating.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations.Biophysical journal · 2014Article
- Agonists binding nicotinic receptors elicit specific channel-opening patterns at αγ and αδ sites.The Journal of physiology · 2014Article
- Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).The Journal of biological chemistry · 2014Article
- The structural mechanism of the Cys-loop receptor desensitization.Molecular neurobiology · 2013Review
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Article
- Size matters in activation/inhibition of ligand-gated ion channels.Trends in pharmacological sciences · 2012Review
- End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Physiological reviews · 2012Review
- The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel.The Journal of general physiology · 2012Article
- The α1K276E startle disease mutation reveals multiple intermediate states in the gating of glycine receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
27 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We used single-channel recording and model-based kinetic analyses to quantify the effects of mutations in the extracellular domain (ECD) of the alpha-subunit of mouse muscle-type acetylcholine receptors (AChRs). The crystal structure of an acetylcholine binding protein (AChBP) suggests that the ECD is comprised of a beta-sandwich core that is surrounded by loops. Here we focus on loops 2 and 7, which lie at the interface of the AChR extracellular and transmembrane domains. Side chain substitutions in these loops primarily affect channel gating by either decreasing or increasing the gating equilibrium constant. Many of the mutations to the beta-core prevent the expression of functional AChRs, but of the mutants that did express almost all had wild-type behavior. Rate-equilibrium free energy relationship analyses reveal the presence of two contiguous, distinct synchronously-gating domains in the alpha-subunit ECD that move sequentially during the AChR gating reaction. The transmitter-binding site/loop 5 domain moves first (Phi = 0.93) and is followed by the loop 2/loop 7 domain (Phi = 0.80). These movements precede that of the extracellular linker (Phi = 0.69). We hypothesize that AChR gating occurs as the stepwise movements of such domains that link the low-to-high affinity conformational change in the TBS with the low-to-high conductance conformational change in the pore.
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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.