ArticleThe Biochemical journal2013
Inter-residue coupling contributes to high-affinity subtype-selective binding of α-bungarotoxin to nicotinic receptors.
Article in The Biochemical journal, 2013. 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.
- An Investigation of Three-Finger Toxin-nAChR Interactions through Rosetta Protein Docking.Toxins · 2020Article
- Structure-Function of Neuronal Nicotinic Acetylcholine Receptor Inhibitors Derived From Natural Toxins.Frontiers in neuroscience · 2020Review
- Structural basis for α-bungarotoxin insensitivity of neuronal nicotinic acetylcholine receptors.Neuropharmacology · 2019Article
- Drysdalin, an antagonist of nicotinic acetylcholine receptors highlights the importance of functional rather than structural conservation of amino acid residues.FASEB bioAdvances · 2019Article
- Receptor variability-driven evolution of snake toxins.Zoological research · 2018Article
- Nicotinic acetylcholine receptors at the single-channel level.British journal of pharmacology · 2018Review
- Molecular function of α7 nicotinic receptors as drug targets.The Journal of physiology · 2018Review
- Differential Contribution of Subunit Interfaces to α9α10 Nicotinic Acetylcholine Receptor Function.Molecular pharmacology · 2017Article
- Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors.Nature communications · 2015Article
- Structural basis for cooperative interactions of substituted 2-aminopyrimidines with the acetylcholine binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Inhibition of nicotinic acetylcholine receptors, a novel facet in the pleiotropic activities of snake venom phospholipases A2.PloS one · 2014Article
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5 authors.
Funding
Abstract
The crystal structure of a pentameric α7 ligand-binding domain chimaera with bound α-btx (α-bungarotoxin) showed that of the five conserved aromatic residues in α7, only Tyr¹⁸⁴ in loop C of the ligand-binding site was required for high-affinity binding. To determine whether the contribution of Tyr¹⁸⁴ depends on local residues, we generated mutations in an α7/5HT(3A) (5-hydroxytryptamine type 3A) receptor chimaera, individually and in pairs, and measured ¹²⁵I-labelled α-btx binding. The results show that mutations of individual residues near Tyr¹⁸⁴ do not affect α-btx affinity, but pairwise mutations decrease affinity in an energetically coupled manner. Kinetic measurements show that the affinity decreases arise through increases in the α-btx dissociation rate with little change in the association rate. Replacing loop C in α7 with loop C from the α-btx-insensitive α2 or α3 subunits abolishes high-affinity α-btx binding, but preserves acetylcholine-elicited single channel currents. However, in both the α2 and α3 construct, mutating either residue that flanks Tyr¹⁸⁴ to its α7 counterpart restores high-affinity α-btx binding. Analogously, in α7, mutating both residues that flank Tyr¹⁸⁴ to the α2 or α3 counterparts abolishes high-affinity α-btx binding. Thus interaction between Tyr¹⁸⁴ and local residues contributes to high-affinity subtype-selective α-btx binding.
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