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

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dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorDo-heyoung Kim-
dc.contributor.authorB M Olivera-
dc.contributor.authorJ M McIntosh-
dc.contributor.authorKyou Hoon Han-
dc.date.accessioned2017-04-19T09:05:17Z-
dc.date.available2017-04-19T09:05:17Z-
dc.date.issued2006-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2006.04.099ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7586-
dc.description.abstractα-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.-
dc.publisherElsevier-
dc.titleSolution conformation of a neuronal nicotinic acetylcholine receptor antagonist α-conotoxin OmIA that discriminates α3 vs. α6 nAChR subtypes-
dc.title.alternativeSolution conformation of a neuronal nicotinic acetylcholine receptor antagonist α-conotoxin OmIA that discriminates α3 vs. α6 nAChR subtypes-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number1-
dc.citation.endPage254-
dc.citation.startPage248-
dc.citation.volume345-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorDo-heyoung Kim-
dc.contributor.affiliatedAuthorKyou Hoon Han-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeNameOlivera-
dc.contributor.alternativeNameMcIntosh-
dc.contributor.alternativeName한규훈-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 345, no. 1, pp. 248-254-
dc.identifier.doi10.1016/j.bbrc.2006.04.099-
dc.subject.keywordα-Conotoxin-
dc.subject.keywordnicotinic acetylcholine receptor-
dc.subject.keywordNMR-
dc.subject.keywordpeptide-
dc.subject.keywordsolution structure-
dc.subject.localα-conotoxin-
dc.subject.localα-Conotoxin-
dc.subject.localnicotinic acetylcholine receptor (nAChR)-
dc.subject.localNicotinic acetylcholine receptors (nAChRs)-
dc.subject.localNicotinic acetylcholine receptor-
dc.subject.localnicotinic acetylcholine receptor-
dc.subject.localNMR-
dc.subject.localnuclear magnetic resonance (Nmr)-
dc.subject.localNuclear magnetic resonance-
dc.subject.localnuclear magnetic resonance-
dc.subject.localNuclear magnetic resonance (NMR)-
dc.subject.localpeptide-
dc.subject.localPeptides-
dc.subject.localPeptide-
dc.subject.localSolution structure-
dc.subject.localsolution structure-
dc.description.journalClassY-
Appears in Collections:
Division of A.I. & Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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