NMR structure determination of α-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold

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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.accessioned2017-04-19T09:05:04Z-
dc.date.available2017-04-19T09:05:04Z-
dc.date.issued2006-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2006.08.164ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7568-
dc.description.abstractWe have determined a high-resolution three-dimensional structure of α-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus bullatus. Despite its unusual 4/4 disulfide bond layout α-conotoxin BuIA exhibits strong antagonistic activity at α6/α3β2β3, α3β2, and α3β4 nAChR subtypes like some α4/7 conotoxins. α-Conotoxin BuIA lacks the C-terminal β-turn present within the second disulfide loop of α4/7 conotoxins, having only a "pseudo ω-shaped" molecular topology. Nevertheless, it contains a functionally critical two-turn helix motif, a feature ubiquitously found in α4/7 conotoxins. Such an aspect seems mainly responsible for similarities in the receptor recognition profile of α-conotoxin BuIA to α4/7 conotoxins. Structural comparison of α-conotoxin BuIA with α4/7 conotoxins and α4/3 conotoxin ImI suggests that presence of the second helical turn portion of the two-turn helix motif in α4/7 and α4/4 conotoxins may be important for binding to the α3 and/or α6 subunit of nAChR.-
dc.publisherElsevier-
dc.titleNMR structure determination of α-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold-
dc.title.alternativeNMR structure determination of α-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number3-
dc.citation.endPage1234-
dc.citation.startPage1228-
dc.citation.volume349-
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. 349, no. 3, pp. 1228-1234-
dc.identifier.doi10.1016/j.bbrc.2006.08.164-
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 Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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