ArticleNature2001
Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors.
Article in Nature, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 632 papers.
What it found
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Who cites it
632 citing papers in PubMed, 1,746 citations in OpenAlex.
- The central cholinergic system as a therapeutic target in Parkinson's disease.Journal of Parkinson's disease · 2026Review
- Drug Discovery Targeting Nicotinic Acetylcholine Receptors for Hearing Loss.International journal of molecular sciences · 2026Review
- Genome-wide analysis reveals pathways important for the development and maturation of excitatory synaptic connections to GABAergic neurons.G3 (Bethesda, Md.) · 2026Article
- Structure of a pH-sensitive pentameric ligand-gated ion channel from the Sarcoptes scabies mite.Nature communications · 2026Article
- RIC-3 Interacts Directly with the 5-HTbioRxiv : the preprint server for biology · 2026Article
- Chimeric Approach to Identify Molecular Determinants of Nicotinic Acetylcholine Receptors.International journal of molecular sciences · 2026Review
- The role of acetylcholine and its receptors in tumor immune regulation: mechanisms and potential therapeutic targets.Molecular cancer · 2025Review
- Dynamics and Interplay of the Binding Pockets in the Glycine Receptor.Journal of chemical information and modeling · 2025Article
- The Cation-π Interaction in Chemistry and Biology.Chemical reviews · 2025Review
- In Silico Conotoxin Studies: Progress and Prospects.Molecules (Basel, Switzerland) · 2024Review
- Unravelling nicotinic receptor and ligand features underlying neonicotinoid knockdown actions on the malaria vector mosquitoOpen biology · 2024Article
- Protein Painting Mass Spectrometry in the Discovery of Interaction Sites within the Acetylcholine Binding Protein.ACS chemical neuroscience · 2024Article
- Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site.Nature communications · 2024Article
- The Cyclic Imine Core Common to the Marine Macrocyclic Toxins Is Sufficient to Dictate Nicotinic Acetylcholine Receptor Antagonism.Marine drugs · 2024Article
- Efficient Expression inMolecules (Basel, Switzerland) · 2024Article
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
- Dual mutations in the whitefly nicotinic acetylcholine receptor β1 subunit confer target-site resistance to multiple neonicotinoid insecticides.PLoS genetics · 2024Article
- Nicotine Motivated Behavior inInternational journal of molecular sciences · 2024Article
- Targeting Alpha7 Nicotinic Acetylcholine Receptors in Lung Cancer: Insights, Challenges, and Therapeutic Strategies.ACS pharmacology & translational science · 2024Review
- Startle Disease: New Molecular Insights into an Old Neurological Disorder.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2023Review
572 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pentameric ligand gated ion-channels, or Cys-loop receptors, mediate rapid chemical transmission of signals. This superfamily of allosteric transmembrane proteins includes the nicotinic acetylcholine (nAChR), serotonin 5-HT3, gamma-aminobutyric-acid (GABAA and GABAC) and glycine receptors. Biochemical and electrophysiological information on the prototypic nAChRs is abundant but structural data at atomic resolution have been missing. Here we present the crystal structure of molluscan acetylcholine-binding protein (AChBP), a structural and functional homologue of the amino-terminal ligand-binding domain of an nAChR alpha-subunit. In the AChBP homopentamer, the protomers have an immunoglobulin-like topology. Ligand-binding sites are located at each of five subunit interfaces and contain residues contributed by biochemically determined 'loops' A to F. The subunit interfaces are highly variable within the ion-channel family, whereas the conserved residues stabilize the protomer fold. This AChBP structure is relevant for the development of drugs against, for example, Alzheimer's disease and nicotine addiction.
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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.