ArticleProceedings of the National Academy of Sciences of the United States of America2007
The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 51 citations in OpenAlex.
- Illuminating High-Affinity ATP Binding to the Sodium-Potassium Pump Using Solid-State NMR Spectroscopy.Molecules (Basel, Switzerland) · 2025Review
- Mass spectrometry imaging reveals new biological roles for choline esters and Tyrian purple precursors in muricid molluscs.Scientific reports · 2015Article
- Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Journal of biomolecular NMR · 2015Article
- Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Physiological reviews · 2012Review
- Anesthetic effects on the structure and dynamics of the second transmembrane domains of nAChR alpha4beta2.Biochimica et biophysica acta · 2010Article
- Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system.Nature reviews. Drug discovery · 2009Review
- Photoaffinity labeling the agonist binding domain of alpha4beta4 and alpha4beta2 neuronal nicotinic acetylcholine receptors with [(125)I]epibatidine and 5[(125)I]A-85380.Biochimica et biophysica acta · 2009Article
- Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements.Chemphyschem : a European journal of chemical physics and physical chemistry · 2009Article
- Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles.Biophysical journal · 2009Article
- Dipolar truncation in magic-angle spinning NMR recoupling experiments.The Journal of chemical physics · 2009Article
- Retinal conformation and dynamics in activation of rhodopsin illuminated by solid-state H NMR spectroscopy.Photochemistry and photobiologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
Abstract
The conformation of the neurotransmitter acetylcholine bound to the fully functional nicotinic acetylcholine receptor embedded in its native membrane environment has been characterized by using frequency-selective recoupling solid-state NMR. Six dipolar couplings among five resolved (13)C-labeled atoms of acetylcholine were measured. Bound acetylcholine adopts a bent conformation characterized with a quaternary ammonium-to-carbonyl distance of 5.1 A. In this conformation, and with its orientation constrained to that previously determined by us, the acetylcholine could be docked satisfactorily in the agonist pocket of the agonist-bound, but not the agonist-free, crystal structure of a soluble acetylcholine-binding protein from Lymnaea stagnali. The quaternary ammonium group of the acetylcholine was determined to be within 3.9 A of five aromatic residues and its acetyl group close to residues C187/188 of the principle and residue L112 of the complementary subunit. The observed >C O chemical shift is consistent with H bonding to the nicotinic acetylcholine receptor residues gammaY116 and deltaT119 that are homologous to L112 in the soluble acetylcholine-binding protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.