Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist α-conotoxin OmIA that discriminates α3 vs. α6 nAChR subtypes

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Title
Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist α-conotoxin OmIA that discriminates α3 vs. α6 nAChR subtypes
Author(s)
Seung-Wook ChiDo-heyoung Kim; B M Olivera; J M McIntosh; Kyou Hoon Han
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 345, no. 1, pp. 248-254
Publication Year
2006
Abstract
α-Conotoxin OmIA from Conus omaria is the only α-conotoxin that shows a ∼20-fold higher affinity to the α3β2 over the α6β2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of α-conotoxin OmIA by nuclear magnetic resonance spectroscopy. α-Conotoxin OmIA has an "ω-shaped" overall topology with His5-Asn12 forming an α-helix. Structural features of α-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related α4/7 subfamily conotoxins. Reduced size of the hydrophilic area in α-conotoxin OmIA seems to be associated with the reduced affinity towards the α6β2 nAChR subtype.
Keyword
α-Conotoxinnicotinic acetylcholine receptorNMRpeptidesolution structure
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2006.04.099
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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