ArticleThe Journal of physiology2002
Contributions of the non-alpha subunit residues (loop D) to agonist binding and channel gating in the muscle nicotinic acetylcholine receptor.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Chimeric Approach to Identify Molecular Determinants of Nicotinic Acetylcholine Receptors.International journal of molecular sciences · 2026Review
- Article
- Differential Contribution of Subunit Interfaces to α9α10 Nicotinic Acetylcholine Receptor Function.Molecular pharmacology · 2017Article
- Synaptic-type α1β2γ2L GABAA receptors produce large persistent currents in the presence of ambient GABA and anesthetic drugs.Molecular pharmacology · 2015Article
- γ-aminobutyric acid type A α4, β2, and δ subunits assemble to produce more than one functionally distinct receptor type.Molecular pharmacology · 2014Article
- α1F64 Residue at GABA(A) receptor binding site is involved in gating by influencing the receptor flipping transitions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- The benzodiazepine diazepam potentiates responses of α1β2γ2L γ-aminobutyric acid type A receptors activated by either γ-aminobutyric acid or allosteric agonists.Anesthesiology · 2013Article
- Energetic contributions to channel gating of residues in the muscle nicotinic receptor β1 subunit.PloS one · 2013Article
- Highly fatal fast-channel syndrome caused by AChR ε subunit mutation at the agonist binding site.Neurology · 2012Article
- Functional characterization of the α5(Asn398) variant associated with risk for nicotine dependence in the α3β4α5 nicotinic receptor.Molecular pharmacology · 2011Article
- Design and control of acetylcholine receptor conformational change.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Crystal structures of a cysteine-modified mutant in loop D of acetylcholine-binding protein.The Journal of biological chemistry · 2011Article
- Energetics of gating at the apo-acetylcholine receptor transmitter binding site.The Journal of general physiology · 2010Article
- Structural basis of activation of cys-loop receptors: the extracellular-transmembrane interface as a coupling region.Molecular neurobiology · 2009Review
- Hydrogen bonding between the 17beta-substituent of a neurosteroid and the GABA(A) receptor is not obligatory for channel potentiation.British journal of pharmacology · 2009Article
- 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
- Aromatic Residues {epsilon}Trp-55 and {delta}Trp-57 and the Activation of Acetylcholine Receptor Channels.The Journal of biological chemistry · 2009Article
- The 5-HT3 receptor--the relationship between structure and function.Neuropharmacology · 2009Review
- Activation and block of the adult muscle-type nicotinic receptor by physostigmine: single-channel studies.Molecular pharmacology · 2008Article
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1 author.
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Abstract
The agonist binding site of the nicotinic acetylcholine receptor has a loop-based structure, and is formed by residues located remotely to each other in terms of primary structure. Amino acid residues in sites delta57 and delta59, and the equivalent residues in the epsilon; subunit, have been identified as part of the agonist binding site and designated as loop D. The effects of point mutations in sites delta57, delta59, epsilon;55 and epsilon;57 on agonist binding and channel gating were studied. The mutated receptors were expressed transiently in HEK 293 cells and the currents were recorded using the cell-attached single-channel patch clamp technique. The results demonstrate that the mutations mainly affect channel gating with the major portion of the effect due to a reduction in the channel opening rate constant. For both the delta57/epsilon;55 and the delta59/epsilon;57 site, a mutation in the epsilon; subunit had a greater effect on channel gating than a mutation in the delta subunit. In all instances, agonist binding was affected to a lesser degree than channel gating. Previous data have placed the delta57 and delta59 residues in or near the agonist binding pocket. The data presented here suggest that these two residues (and the homologous sites in the epsilon; subunit) are not involved in specific interactions with the nicotinic agonist and that they affect the activation of the nicotinic receptor by shaping the overall structure of the agonist binding site.
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