Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus

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dc.contributor.authorSi Hyung Lee-
dc.contributor.authorEun Ji Cha-
dc.contributor.authorJ E Lim-
dc.contributor.authorS H Kwon-
dc.contributor.authorDo Hyoung Kim-
dc.contributor.authorH Cho-
dc.contributor.authorKyou Hoon Han-
dc.date.accessioned2017-04-19T09:33:27Z-
dc.date.available2017-04-19T09:33:27Z-
dc.date.issued2012-
dc.identifier.issn10168478-
dc.identifier.uri10.1007/s10059-012-0060-zko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10902-
dc.description.abstractThe hepatitis B virus x protein (HBX) is expressed in HBVinfected liver cells and can interact with a wide range of cellular proteins. In order to understand such promiscuous behavior of HBX we expressed a truncated mini-HBX protein (named Tr-HBX) (residues 18-142) with 5 Cys?Ser mutations and characterized its structural features using circular dichroism (CD) spectropolarimetry, NMR spectroscopy as well as bioinformatics tools for predicting disorder in intrinsically unstructured proteins (IUPs). The secondary structural content of Tr-HBX from CD data suggests that Tr-HBX is only partially folded. The protein disorder prediction by IUPred reveals that the unstructured region encompasses its N-Terminal ?30 residues of Tr-HBX. A two-dimensional 1H- 15N HSQC NMR spectrum exhibits fewer number of resonances than expected, suggesting that Tr-HBX is a hybrid type IUP where its folded Cterminal half coexists with a disordered N-Terminal region. Many IUPs are known to be capable of having promiscuous interactions with a multitude of target proteins. Therefore the intrinsically disordered nature of Tr-HBX revealed in this study provides a partial structural basis for the promiscuous structure-function behavior of HBX.-
dc.publisherSouth Korea-
dc.titleStructural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus-
dc.title.alternativeStructural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number2-
dc.citation.endPage169-
dc.citation.startPage165-
dc.citation.volume34-
dc.contributor.affiliatedAuthorDo Hyoung Kim-
dc.contributor.alternativeName이시형-
dc.contributor.alternativeName차은지-
dc.contributor.alternativeName임지은-
dc.contributor.alternativeName권순환-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeName조혜성-
dc.contributor.alternativeName한규훈-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 34, no. 2, pp. 165-169-
dc.identifier.doi10.1007/s10059-012-0060-z-
dc.subject.keywordCircular dichroism (CD) spectropolarimetry-
dc.subject.keywordHepatitis B virus-X (HBX)-
dc.subject.keywordIntrinsically unstructured/unfolded protein (IUP)-
dc.subject.keywordNuclear magnetic resonance (NMR) spectroscopy-
dc.subject.keywordPromiscuity-
dc.subject.keywordTruncated mini-HBX (Tr-HBX)-
dc.subject.localCircular dichroism (CD) spectropolarimetry-
dc.subject.localHepatitis B virus-X (HBX)-
dc.subject.localHepatitis B virus X (HBx)-
dc.subject.localIntrinsically unstructured/unfolded protein (IUP)-
dc.subject.localNuclear magnetic resonance (NMR) spectroscopy-
dc.subject.localPromiscuity-
dc.subject.localTruncated mini-HBX (Tr-HBX)-
dc.description.journalClassY-
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Division of Bio Technology Innovation > Core Facility Management Center > 1. Journal Articles
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