Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1939354 | Biochemical and Biophysical Research Communications | 2006 | 7 Pages |
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.
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Authors
Seung-Wook Chi, Do-Hyoung Kim, Baldomero M. Olivera, J. Michael McIntosh, Kyou-Hoon Han,