Characterization of a human α₁-antitrypsin variant that is as stable as ovalbumin

Cited 31 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorKee Nyung Lee-
dc.contributor.authorHa Na Im-
dc.contributor.authorSang Won Kang-
dc.contributor.authorMyeong Hee Yu-
dc.date.accessioned2017-04-19T08:55:45Z-
dc.date.available2017-04-19T08:55:45Z-
dc.date.issued1998-
dc.identifier.issn00219258-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4577-
dc.description.abstractThe metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role in the facile conformational switch and the insertion of the reactive center loop into the central β-sheet, A-sheet, during the formation of a stable complex between a serpin and its target proteinase. We have examined the folding and inhibitory activity of a very stable variant of human α1-antitrypsin, a prototype inhibitory serpin. A combination of seven stabilizing single amino acid substitutions of α1- antitrypsin, designated Multi-7, increased the midpoint of the unfolding transition to almost that of ovalbumin, a non-inhibitory but more stable serpin. Compared with the wild-type α1-antitrypsin, Multi-7 retarded the opening of A-sheet significantly, as revealed by the retarded unfolding and latency conversion of the native state. Surprisingly, Multi-7 α1- antitrypsin could form a stable complex with a target elastase with the same kinetic parameters and the stoichiometry of inhibition as the wild type, indicating that enhanced A-sheet closure conferred by Multi-7 does not affect the complex formation. It may be that the stability increase of Multi-7 α1- antitrypsin is not sufficient to influence the rate of loop insertion during the complex formation.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleCharacterization of a human α₁-antitrypsin variant that is as stable as ovalbumin-
dc.title.alternativeCharacterization of a human α₁-antitrypsin variant that is as stable as ovalbumin-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number5-
dc.citation.endPage2516-
dc.citation.startPage2509-
dc.citation.volume273-
dc.contributor.alternativeName이기녕-
dc.contributor.alternativeName임하나-
dc.contributor.alternativeName강상원-
dc.contributor.alternativeName유명희-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 273, no. 5, pp. 2509-2516-
dc.identifier.doi10.1074/jbc.273.5.2509-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.