ArticleNeuropharmacology2019
Structural basis for α-bungarotoxin insensitivity of neuronal nicotinic acetylcholine receptors.
Article in Neuropharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Early effects of α7nAChR regulation on maxillary expansion in mice : A study on osteogenesis and inflammatory factors.Journal of orofacial orthopedics = Fortschritte der Kieferorthopadie : Organ/official journal Deutsche Gesellschaft fur Kieferorthopadie · 2026Article
- Protective effects of clinical anticholinergic and anticholinesterase agents against Bungarus multicinctus venom and neurotoxin-rich snake venoms.PLoS neglected tropical diseases · 2025Article
- Cluster FLISA-A Method to Compare Protein Expression Efficiency Between Cell Lines and Subunit Clustering of Proteins.Bio-protocol · 2025Article
- N-Glycosylation Deficiency in Transgene α7 nAChR and RIC3 Expressing CHO Cells Without NACHO.The Journal of membrane biology · 2024Article
- The molecular mechanism of snake short-chain α-neurotoxin binding to muscle-type nicotinic acetylcholine receptors.Nature communications · 2022Article
- Probing function in ligand-gated ion channels without measuring ion transport.The Journal of general physiology · 2022Article
- Network Pharmacological Study on the Mechanism of Cynanchum paniculatum (Xuchangqing) in the Treatment of Bungarus multicinctus Bites.BioMed research international · 2022Article
- Compensatory mechanisms in resistant Anopheles gambiae AcerKis and KdrKis neurons modulate insecticide-based mosquito control.Communications biology · 2021Article
- Article
- Mechanism of calcium potentiation of the α7 nicotinic acetylcholine receptor.The Journal of general physiology · 2020Article
- Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins.Neuron · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ten types of nicotinic acetylcholine receptor α-subunits show substantial sequence homology, yet some types confer high affinity for α-bungarotoxin, whereas others confer negligible affinity. Combining sequence alignments with structural data reveals three residues unique to α-toxin-refractory α-subunits that coalesce within the 3D structure of the α4β2 receptor and are predicted to fit between loops I and II of α-bungarotoxin. Mutating any one of these residues, Lys189, Ile196 or Lys153, to the α-toxin-permissive counterpart fails to confer α-bungarotoxin binding. However, mutating both Lys189 and Ile196 affords α-bungarotoxin binding with an apparent dissociation constant of 104 nM, while combining mutation of Lys153 reduces the dissociation constant to 22 nM. Analogous residue substitutions also confer high affinity α-bungarotoxin binding upon α-toxin-refractory α2 and α3 subunits. α4β2 receptors engineered to bind α-bungarotoxin exhibit slow rates of α-toxin association and dissociation, and competition by cholinergic ligands typical of muscle nicotinic receptors. Receptors engineered to bind α-bungarotoxin co-sediment with muscle nicotinic receptors on sucrose gradients, and mirror single channel signatures of their α-toxin-refractory counterparts. Thus the inability of α-bungarotoxin to bind to neuronal nicotinic receptors arises from three unique and interdependent residues that coalesce within the receptor's 3D structure.
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