Solution conformation of α-conotoxin GIC, a novel potent antagonist of α3β2 nicotinic acetylcholine receptors

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Title
Solution conformation of α-conotoxin GIC, a novel potent antagonist of α3β2 nicotinic acetylcholine receptors
Author(s)
Seung-Wook ChiDo-Hyoung Kim; B M Olivera; J M McIntosh; Kyou Hoon Han
Bibliographic Citation
Biochemical Journal, vol. 380, no. 2, pp. 347-352
Publication Year
2004
Abstract
α-Conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. α-Conotoxin GIC potently blocks the α3β2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of α-conotoxin GIC by NMR spectroscopy. The structure of α-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 ? and 0.96 ? respectively. Structure and surface comparison of α-conotoxin GIC with the other α4/7 subfamily conotoxins reveals unique structural aspects of α-conotoxin GIC. In particular, the structural comparison between α-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of α-conotoxin GIC.
Keyword
α-conotoxinconus geographus (cone snail)nicotinic acetylcholine receptor (nAChR)NMRsolution structurevenom
ISSN
0264-6021
Publisher
Portland Press Ltd
DOI
http://dx.doi.org/10.1042/BJ20031792
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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