Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
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Summary
The crystal structure of molluscan acetylcholine-binding protein (AChBP), a structural and functional homologue of the amino-terminal ligand-binding domain of an nAChR α-subunit, is presented and is relevant for the development of drugs against Alzheimer’s disease and nicotine addiction.
- Type
- article
- Published
- 2001-05-17
- Cited by
- 1,755
- References
- 55
- OpenAlex
- https://openalex.org/W1788430178
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4415937
Keywords
Cys-loop receptors, Allosteric regulation, Ligand-gated ion channel, Nicotinic agonist, Ion channel
References
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- Improved methods for building protein models in electron density maps and the location of errors in these models.
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Cited by
- Fluorescence Studies of the Acetylcholine Receptor: Structure and Dynamics in Membranes and Cells
- Chemical scale investigations of ligand-gated ion channels using unnatural amino acids
- Inhibitory Glycine Receptors: An
- Identification of critical residues in loop E in the 5-HT3ASR binding site
- AFFINITY LABELING OF CYSTEINE-MUTANTS EVIDENCES CONTACT RESIDUES IN MODELED RECEPTOR BINDING SITES
- Acetylcholine Receptors Direct Rapsyn Clusters to the Neuromuscular Synapse in Zebrafish
- Escobar syndrome is a prenatal myasthenia caused by disruption of the acetylcholine receptor fetal gamma subunit.
- GABA(A) receptor mutations associated with generalized epilepsies.
- The role of protein 3D-structures in the drug discovery process.
- Insights into docking and scoring neuronal α4β2 nicotinic receptor agonists using molecular dynamics simulations and QM/MM calculations
- Molecular determinants of β‐carboline inhibition of the glycine receptor
- Nicotine-induced human breast cancer cell proliferation attenuated by garcinol through down-regulation of the nicotinic receptor and cyclin D3 proteins
- α-Conotoxin AuIB Isomers Exhibit Distinct Inhibitory Mechanisms and Differential Sensitivity to Stoichiometry of α3β4 Nicotinic Acetylcholine Receptors*
- A residue close to α1 loop F disrupts modulation of GABAA receptors by benzodiazepines while their binding is maintained
- Insights into the structure and pharmacology of GABA(A) receptors.
- Charakterisierung der Interaktion von Gephyrin mit verschiedenen Untereinheiten des GABAA-Rezeptors
- Discovery of a novel alpha-7 nicotinic acetylcholine receptor agonist series and characterization of the potent, selective, and orally efficacious agonist 5-(4-acetyl[1,4]diazepan-1-yl)pentanoic acid [5-(4-methoxyphenyl)-1H-pyrazol-3-yl] amide (SEN15924, WAY-361789).
- Molecular basis for the differential sensitivity of rat and human α9α10 nAChRs to α-conotoxin RgIA
- Exploring the orthosteric binding site of the γ-aminobutyric acid type A receptor using 4-(Piperidin-4-yl)-1-hydroxypyrazoles 3- or 5-imidazolyl substituted: design, synthesis, and pharmacological evaluation.
- Covalent Trapping of Methyllycaconitine at the α4-α4 Interface of the α4β2 Nicotinic Acetylcholine Receptor
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