| 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 |
©American Society for Biochemistry and Molecular Biology |
| 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 |
