Identification of a New Component of the Agonist Binding Site of the Nicotinic 7 Homooligomeric Receptor (*)
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Summary
Data support the participation of Trp-54 to ligand binding, and provide evidence for a new “complementary component” of the α7 nicotinic binding site, distinct from its three-loop “principal component,” and homologous to the “non-α component’ present on and subunits.
- Type
- article
- Published
- 1995-05-19
- Cited by
- 142
- References
- 28
- Access
- Open access
- OpenAlex
- https://openalex.org/W2013341464
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24306712
Keywords
Agonist, Identification (biology), Nicotinic agonist, Component (thermodynamics), Receptor
References
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- Identification of a [3H]muscimol photoaffinity substrate in the bovine gamma-aminobutyric acidA receptor alpha subunit.
- Both alpha- and beta-subunits contribute to the agonist sensitivity of neuronal nicotinic acetylcholine receptors
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- High-efficiency transformation of mammalian cells by plasmid DNA.
- A neuronal nicotinic acetylcholine receptor subunit (alpha 7) is developmentally regulated and forms a homo-oligomeric channel blocked by alpha-BTX.
- Brain α-bungarotoxin binding protein cDNAs and MAbs reveal subtypes of this branch of the ligand-gated ion channel gene superfamily
- Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non‐identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex
- Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine.
- Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand.
- Neurotransmitter-gated ion channels as unconventional allosteric proteins
- Chimaeric nicotinic–serotonergic receptor combines distinct ligand binding and channel specificities
- Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor.
- Molecular Dissection of Subunit Interfaces in the Acetylcholine Receptor
- Functional significance of aromatic amino acids from three peptide loops of the α7 neuronal nicotinic receptor site investigated by site‐directed mutagenesis
- Crosslinking of α‐bungarotoxin to the acetylcholine receptor from Torpedo marmorata by ultraviolet light irradiation
- d-Tubocurarine binding sites are located at alpha-gamma and alpha-delta subunit interfaces of the nicotinic acetylcholine receptor.
Cited by
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- Nicotinic acetylcholine receptor-lipid interactions: Mechanistic insight and biological function.
- Nicotinic acetylcholine receptors from the parasitic nematode Ascaris suum
- An invermectin sensitive ion channel from haemonchus contortus.
- Critical Elements Determining Diversity in Agonist Binding and Desensitization of Neuronal Nicotinic Acetylcholine Receptors
- Neuronal α-Bungarotoxin Receptors Differ Structurally from Other Nicotinic Acetylcholine Receptors
- Reviews of Physiology, Biochemistry and Pharmacology
- The nicotinic acetylcholine receptor subunit family expressed in the central nervous system of the freshwater snail Lymnaea stagnalis: Molecular and functional diversity of the neuronal nicotinic acetylcholine receptors in a molluscan species
- Human α4β2 Neuronal Nicotinic Acetylcholine Receptor in HEK 293 Cells: A Patch-Clamp Study
- Investigating the Effects of Anthelmintic Compounds at the Site of Zinc Potentiation on Alpha4Beta4 Neuronal Nicotinic Acetylcholine Receptors
- Assembly and trafficking of nicotinic and 5HT3 receptors.
- Brain nicotinic receptors: structure and regulation, role in learning and reinforcement.
- Ion Channels in Drug Discovery - focus on biological assays
- Neuronal nicotinic acetylcholine receptors.
- Aromatic residues at position 55 of rat α7 nicotinic acetylcholine receptors are critical for maintaining rapid desensitization
- The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor.
- Determinants of Competitive Antagonist Sensitivity on Neuronal Nicotinic Receptor β Subunits
- Neuronal α-Bungarotoxin Receptors Are α7 Subunit Homomers
- Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
- Ultrastructural Localization of the α4-Subunit of the Neuronal Acetylcholine Nicotinic Receptor in the Rat Substantia Nigra
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