Solution Conformation of α-Conotoxin EI, a Neuromuscular Toxin Specific for the α1/δ Subunit Interface of Torpedo Nicotinic Acetylcholine Receptor
| Autor: | William R. Gray, J. Michael McIntosh, Kyou-Hoon Han, Jae Eun Suk, Richard B. Jacobsen, Kyu Hwan Park |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Stereochemistry Molecular Sequence Data Neuromuscular Junction Nicotinic Antagonists Receptors Nicotinic Torpedo complex mixtures Biochemistry law.invention Ganglion type nicotinic receptor law Muscarinic acetylcholine receptor M5 Animals Amino Acid Sequence Disulfides Conotoxin Nuclear Magnetic Resonance Biomolecular Molecular Biology Acetylcholine receptor Chemistry Cell Biology musculoskeletal system Protein Structure Tertiary Nicotinic acetylcholine receptor Nicotinic agonist nervous system Alpha-4 beta-2 nicotinic receptor Conotoxins Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 276:49028-49033 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m107798200 |
| Popis: | A high resolution structure of alpha-conotoxin EI has been determined by (1)H NMR spectroscopy and molecular modeling. alpha-Conotoxin EI has the same disulfide framework as alpha 4/7 conotoxins targeting neuronal nicotinic acetylcholine receptors but antagonizes the neuromuscular receptor as do the alpha 3/5 and alpha A conotoxins. The unique binding preference of alpha-conotoxin EI to the alpha(1)/delta subunit interface of Torpedo neuromuscular receptor makes it a valuable structural template for superposition of various alpha-conotoxins possessing distinct receptor subtype specificities. Structural comparison of alpha-conotoxin EI with the gamma-subunit favoring alpha-conotoxin GI suggests that the Torpedo delta-subunit preference of the former originates from its second loop. Superposition of three-dimensional structures of seven alpha-conotoxins reveals that the estimated size of the toxin-binding pocket in nicotinic acetylcholine receptor is approximately 20 A (height) x 20 A (width) x 15 A (thickness). |
| Databáze: | OpenAIRE |
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