ReviewThe Journal of physiology2010
The gating isomerization of neuromuscular acetylcholine receptors.
Review in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Evaluating sequential and allosteric activation models in IKs channels with mutated voltage sensors.The Journal of general physiology · 2024Article
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
- More than Smoke and Patches: The Quest for Pharmacotherapies to Treat Tobacco Use Disorder.Pharmacological reviews · 2020Review
- Potassium channels in the heart: structure, function and regulation.The Journal of physiology · 2017Review
- Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- An Electrostatic Funnel in the GABA-Binding Pathway.PLoS computational biology · 2016Article
- Functional studies cast light on receptor states.Trends in pharmacological sciences · 2015Review
- Subunit interfaces contribute differently to activation and allosteric modulation of neuronal nicotinic acetylcholine receptors.Neuropharmacology · 2015Article
- Correlating structural and energetic changes in glycine receptor activation.The Journal of biological chemistry · 2015Article
- Atomistic insights into human Cys-loop receptors by solution NMR.Biochimica et biophysica acta · 2015Article
- Article
- Agonists binding nicotinic receptors elicit specific channel-opening patterns at αγ and αδ sites.The Journal of physiology · 2014Article
- ELIC-α7 Nicotinic acetylcholine receptor (α7nAChR) chimeras reveal a prominent role of the extracellular-transmembrane domain interface in allosteric modulation.The Journal of biological chemistry · 2014Article
- Allosteric regulation of pentameric ligand-gated ion channels: an emerging mechanistic perspective.Channels (Austin, Tex.) · 2014Review
- Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes.Quarterly reviews of biophysics · 2013Review
- The additional ACh binding site at the α4(+)/α4(-) interface of the (α4β2)2α4 nicotinic ACh receptor contributes to desensitization.British journal of pharmacology · 2013Article
- Asymmetric transmitter binding sites of fetal muscle acetylcholine receptors shape their synaptic response.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The structural mechanism of the Cys-loop receptor desensitization.Molecular neurobiology · 2013Review
- Specificity of intersubunit general anesthetic-binding sites in the transmembrane domain of the human α1β3γ2 γ-aminobutyric acid type A (GABAA) receptor.The Journal of biological chemistry · 2013Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetylcholine receptor-channels are allosteric proteins that isomerize ('gate') between conformations that have a low vs. high affinity for the transmitter and conductance for ions. In order to comprehend the mechanism by which the affinity and conductance changes are linked it is of value to know the magnitude, timing and distribution of energy flowing through the system. Knowing both the di- and unliganded gating equilibrium constants (E(2) and E(0)) is a foundation for understanding the AChR gating mechanism and for engineering both the ligand and the protein to operate in predictable ways. In adult mouse neuromuscular receptors activated by acetylcholine, E(2) = 28 and E(0) approximately 6.5 x 10(7). At each (equivalent) transmitter binding site acetylcholine provides approximately 5.2 kcal mol(1) to motivate the isomerization. The partial agonist choline provides approximately 3.3 kcal mol(1). The relative time of a residue's gating energy change is revealed by the slope of its rate-equilibrium constant relationship. A map of this parameter suggests that energy propagates as a conformational cascade between the transmitter binding sites and the gate region. Although gating energy changes are widespread throughout the protein, some residues are particularly sensitive to perturbations. Several specific proposals for the structural events that comprise the gating conformational cascade are discussed.
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