ArticleBiophysical journal1999
A mutational analysis of the acetylcholine receptor channel transmitter binding site.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Article
- (+)-Catharanthine potentiates the GABABiochemical pharmacology · 2022Article
- Crystal structure of a human neuronal nAChR extracellular domain in pentameric assembly: Ligand-bound α2 homopentamer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.PloS one · 2014Article
- End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Physiological reviews · 2012Review
- Evidence for an extended hydrogen bond network in the binding site of the nicotinic receptor: role of the vicinal disulfide of the alpha1 subunit.The Journal of biological chemistry · 2011Article
- Energetics of gating at the apo-acetylcholine receptor transmitter binding site.The Journal of general physiology · 2010Article
- Allosteric activation mechanism of the cys-loop receptors.Acta pharmacologica Sinica · 2009Review
- Long-range coupling in an allosteric receptor revealed by mutant cycle analysis.Biophysical journal · 2009Article
- An intersubunit hydrogen bond in the nicotinic acetylcholine receptor that contributes to channel gating.The Journal of biological chemistry · 2008Article
- A hydrogen bond in loop A is critical for the binding and function of the 5-HT3 receptor.Biochemistry · 2008Article
- Acetylcholine receptor gating: movement in the alpha-subunit extracellular domain.The Journal of general physiology · 2007Article
- Conformational dynamics of the alphaM3 transmembrane helix during acetylcholine receptor channel gating.Biophysical journal · 2007Article
- Roles of amino acids and subunits in determining the inhibition of nicotinic acetylcholine receptors by competitive antagonists.Anesthesiology · 2007Article
- A human congenital myasthenia-causing mutation (epsilon L78P) of the muscle nicotinic acetylcholine receptor with unusual single channel properties.The Journal of physiology · 2005Article
- Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding.The Journal of general physiology · 2004Article
- Gating dynamics of the acetylcholine receptor extracellular domain.The Journal of general physiology · 2004Article
- The role of loop 5 in acetylcholine receptor channel gating.The Journal of general physiology · 2003Article
- Activation and block of mouse muscle-type nicotinic receptors by tetraethylammonium.The Journal of physiology · 2003Article
- Contributions of the non-alpha subunit residues (loop D) to agonist binding and channel gating in the muscle nicotinic acetylcholine receptor.The Journal of physiology · 2002Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Mutagenesis and single-channel kinetic analysis were used to investigate the roles of four acetylcholine receptor channel (AChR) residues that are candidates for interacting directly with the agonist. The EC50 of the ACh dose-response curve was increased following alpha-subunit mutations Y93F and Y198F and epsilon-subunit mutations D175N and E184Q. Single-channel kinetic modeling indicates that the increase was caused mainly by a reduced gating equilibrium constant (Theta) in alphaY198F and epsilonD175N, by an increase in the equilibrium dissociation constant for ACh (KD) and a reduction in Theta in alphaY93F, and only by a reduction in KD in epsilonE184Q. This mutation altered the affinity of only one of the two binding sites and was the only mutation that reduced competition by extracellular K+. Additional mutations of epsilonE184 showed that K+ competition was unaltered in epsilonE184D and was virtually eliminated in epsilonE184K, but that neither of these mutations altered the intrinsic affinity for ACh. Thus there is an apparent electrostatic interaction between the epsilonE184 side chain and K+ ( approximately 1.7kBT), but not ACh+. The results are discussed in terms of multisite and induced-fit models of ligand binding to the AChR.
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