Solution conformation of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus
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- Solution conformation of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus
- Seung-Wook Chi; K H Park; Jae Eun Suk; B M Olivera; J M McIntosh; Kyou Hoon Han
- Bibliographic Citation
- Journal of Biological Chemistry, vol. 278, no. 43, pp. 42208-42213
- Publication Year
- 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/αA-family 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 ?. The second domain formed by residues His12-Hyp21 is extremely well defined with a backbone root mean square deviation of 0.52 ?, thus forming a sturdy stem for the entire molecule. The third C-terminal domain formed by residues Hyp22-Gly29 shows an intermediate structural order having a backbone root mean square deviation of 1.04 ?. A structurally ill-defined N-terminal first loop domain connected to a rigid central molecular stem seems to be the general structural feature of the αA-conotoxin subfamily. A detailed structural comparison between αA-conotoxin EIVA and αA-conotoxin PIVA suggests that the higher receptor affinity of αA-conotoxin EIVA than αA-conotoxin PIVA might originate from different steric disposition and charge distribution in the second loop "handle" motif.
- Amer Soc Biochemistry Molecular Biology Inc
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- Division of Biomedical Research > 1. Journal Articles
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