ArticleThe Journal of general physiology2010
Energetics of gating at the apo-acetylcholine receptor transmitter binding site.
Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
- Cyclic activation of endplate acetylcholine receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Molecular recognition at cholinergic synapses: acetylcholine versus choline.The Journal of physiology · 2017Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- Modal affinities of endplate acetylcholine receptors caused by loop C mutations.The Journal of general physiology · 2015Article
- Agonist activation of a nicotinic acetylcholine receptor.Neuropharmacology · 2015Review
- Function of the M1 π-helix in endplate receptor activation and desensitization.The Journal of physiology · 2015Article
- Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations.Biophysical journal · 2014Article
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Function of interfacial prolines at the transmitter-binding sites of the neuromuscular acetylcholine receptor.The Journal of biological chemistry · 2013Article
- An outline of desensitization in pentameric ligand-gated ion channel receptors.Cellular and molecular life sciences : CMLS · 2013Review
- Loop C and the mechanism of acetylcholine receptor-channel gating.The Journal of general physiology · 2013Article
- Thermal unfolding of a mammalian pentameric ligand-gated ion channel proceeds at consecutive, distinct steps.The Journal of biological chemistry · 2013Article
- Energy for wild-type acetylcholine receptor channel gating from different choline derivatives.Biophysical journal · 2013Article
- Article
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Sources of energy for gating by neurotransmitters in acetylcholine receptor channels.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel.The Journal of general physiology · 2012Article
- Thinking in cycles: MWC is a good model for acetylcholine receptor-channels.The Journal of physiology · 2012Article
- Design and control of acetylcholine receptor conformational change.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Acetylcholine receptor channels switch between conformations that have a low versus high affinity for the transmitter and conductance for ions (R<-->R*; gating). The forward isomerization, which begins at the transmitter binding sites and propagates approximately 50 A to the narrow region of the pore, occurs by approximately the same sequence of molecular events with or without agonists present at the binding sites. To pinpoint the forces that govern the R versus R* agonist affinity ratio, we measured single-channel activation parameters for apo-receptors having combinations of mutations of 10 transmitter binding site residues in the alpha (Y93, G147, W149, G153, Y190, C192, and Y198), epsilon (W55 and P121), or delta (W57) subunit. Gating energy changes were largest for the tryptophan residues. The alphaW149 energy changes were coupled with those of the other aromatic amino acids. Mutating the aromatic residues to Phe reduces the R/R* equilibrium dissociation constant ratio, with alphaY190 and alphaW149 being the most sensitive positions. Most of the mutations eliminated long-lived spontaneous openings. The results provide a foundation for understanding how ligands trigger protein conformational change.
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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.