Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the α₁/δ subunit interface of Torpedo nicotinic acetylcholine receptor
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- Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the α₁/δ subunit interface of Torpedo nicotinic acetylcholine receptor
- Kyu Hwan Park; Jae Eun Suk; Richard Jacobsen; William R Gray; J Michael McIntosh; Kyou Hoon Han
- Bibliographic Citation
- Journal of Biological Chemistry, vol. 276, no. 52, pp. 49028-49033
- Publication Year
- A high resolution structure of α-conotoxin EI has been determined by 1H NMR spectroscopy and molecular modeling. α-Conotoxin EI has the same disulfide framework as α4/7 conotoxins targeting neuronal nicotinic acetylcholine receptors but antagonizes the neuromuscular receptor as do the α3/5 and αA conotoxins. The unique binding preference of α-conotoxin EI to the α1/δ subunit interface of Torpedo neuromuscular receptor makes it a valuable structural template for superposition of various α-conotoxins possessing distinct receptor subtype specificities. Structural comparison of α-conotoxin EI with the γ-subunit favoring α-conotoxin GI suggests that the Torpedo α-subunit preference of the former originates from its second loop. Superposition of three-dimensional structures of seven α-conotoxins reveals that the estimated size of the toxin-binding pocket in nicotinic acetylcholine receptor is ∼20 ? (height) × 20 ? (width) × 15 ? (thickness).
- Amer Soc Biochemistry Molecular Biology Inc
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- 1. Journal Articles > Journal Articles
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