ArticleThe Journal of biological chemistry2008
An intersubunit hydrogen bond in the nicotinic acetylcholine receptor that contributes to channel gating.
Article in The Journal of biological chemistry, 2008. 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.
- Targeted Mutations Activate Allosteric Modulation of α5-Containing Nicotinic Acetylcholine Receptors.ACS chemical neuroscience · 2026Article
- A single main-chain hydrogen bond required to keep GABANature communications · 2025Article
- Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.American journal of physiology. Heart and circulatory physiology · 2020Article
- Cadmium opens GluK2 kainate receptors with cysteine substitutions at the M3 helix bundle crossing.The Journal of general physiology · 2019Article
- The connexin26 human mutation N14K disrupts cytosolic intersubunit interactions and promotes channel opening.The Journal of general physiology · 2019Article
- 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
- In Vivo Biosynthesis of a β-Amino Acid-Containing Protein.Journal of the American Chemical Society · 2016Article
- Functional evaluation of key interactions evident in the structure of the eukaryotic Cys-loop receptor GluCl.ACS chemical biology · 2014Article
- In vivo incorporation of non-canonical amino acids by using the chemical aminoacylation strategy: a broadly applicable mechanistic tool.Chembiochem : a European journal of chemical biology · 2014Review
- Functional probes of drug-receptor interactions implicated by structural studies: Cys-loop receptors provide a fertile testing ground.Journal of medicinal chemistry · 2014Review
- Insights on the mechanisms of Ca(2+) regulation of connexin26 hemichannels revealed by human pathogenic mutations (D50N/Y).The Journal of general physiology · 2013Article
- Experimental determination of the vertical alignment between the second and third transmembrane segments of muscle nicotinic acetylcholine receptors.Journal of neurochemistry · 2013Article
- Binding interactions with the complementary subunit of nicotinic receptors.The Journal of biological chemistry · 2013Article
- Molecular determinants of subtype-selective efficacies of cytisine and the novel compound NS3861 at heteromeric nicotinic acetylcholine receptors.The Journal of biological chemistry · 2013Article
- Functionally important aromatic-aromatic and sulfur-π interactions in the D2 dopamine receptor.Journal of the American Chemical Society · 2012Article
- Synaptic neurotransmitter-gated receptors.Cold Spring Harbor perspectives in biology · 2012Review
- Using mutant cycle analysis to elucidate long-range functional coupling in allosteric receptors.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Isoflurane alters the structure and dynamics of GLIC.Biophysical journal · 2011Article
- A tight coupling between β₂Y97 and β₂F200 of the GABA(A) receptor mediates GABA binding.Journal of neurochemistry · 2011Article
- 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
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Authors and funding
4 authors.
Funding
Abstract
The muscle nicotinic acetylcholine receptor is a large, allosteric, ligand-gated ion channel with the subunit composition alpha2betagammadelta. Although much is now known about the structure of the binding site, relatively little is understood about how the binding event is communicated to the channel gate, causing the pore to open. Here we identify a key hydrogen bond near the binding site that is involved in the gating pathway. Using mutant cycle analysis with the novel unnatural residue alpha-hydroxyserine, we find that the backbone N-H of alphaSer-191 in loop C makes a hydrogen bond to an anionic side chain of the complementary subunit upon agonist binding. However, the anionic partner is not the glutamate predicted by the crystal structures of the homologous acetylcholine-binding protein. Instead, the hydrogen-bonding partner is the extensively researched aspartate gammaAsp-174/deltaAsp-180, which had originally been identified as a key binding residue for cationic agonists.
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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.