Solution structure of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus

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Publication Type Journal Article
School or College College of Science
Department Biology
Creator Olivera, Baldomero M.; McIntosh, J. Michael
Other Author Chi, Seung-Wook; Park, Kyu-Hwan; Suk, Jae-Eun; Han, Kyou-Hoon
Title Solution structure of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus
Date 2003
Description We report the solution three-dimensional structure of an αA-conotoxin EIVA determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. The αA-conotoxin EIVA consists of 30 amino acids representing the largest peptide among the α/αAfamily conotoxins discovered so far and targets the neuromuscular nicotinic acetylcholine receptor with high affinity. αA-Conotoxin EIVA consists of three distinct structural domains. The first domain is mainly composed of the Cys3-Cys11-disulfide loop and is structurally ill-defined with a large backbone root mean square deviation of 1.91 Å.
Type Text
Publisher American Society for Biochemistry and Molecular Biology (ASBMB)
First Page 42208
Last Page 42213
Subject Conotoxins; A-conotoxin EIVA; Conus ermineus
Subject LCSH Conus; Marine toxins; Nicotinic receptors -- Antagonists; Neuromuscular blocking agents
Language eng
Bibliographic Citation Chi, S. W., Park, K. H., Suk, J. E., Olivera, B. M., McIntosh, J. M., & Han, K. H. (2003). Solution structure of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus. Journal of Biological Chemistry, 278, 42208-13.
Rights Management (c)American Society for Biochemistry and Molecular Biology (ASBMB) http://www.asbmb.org/
Format Medium application/pdf
Format Extent 378,001 bytes
Identifier ir-main,8428
ARK ark:/87278/s6c25dxk
Setname ir_uspace
ID 706134
Reference URL https://collections.lib.utah.edu/ark:/87278/s6c25dxk
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