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Title 

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

Authors 

Seung-Wook ChiDo-heyoung KimB M OliveraJ M McIntoshKyou Hoon Han

Publisher 

Elsevier

Issue Date 

2006

Citation 

Biochemical and Biophysical Research Communications, vol. 345, no. 1, pp. 248-254

Keywords 

α-Conotoxinnicotinic acetylcholine receptorNMRpeptidesolution structurealpha conotoxin OmIAasparaginenicotinic receptornicotinic receptor alpha3nicotinic receptor alpha6

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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2006.04.099

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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