106 258

Cited 10 times in

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

DC Field Value Language
dc.contributor.authorLee, SH-
dc.contributor.authorCha, EJ-
dc.contributor.authorLim, JE-
dc.contributor.authorKwon, SH-
dc.contributor.authorKim, DH-
dc.contributor.authorCho, H-
dc.contributor.authorHan, KH-
dc.date.accessioned2013-04-22T06:52:44Z-
dc.date.available2013-04-22T06:52:44Z-
dc.date.issued2012-
dc.identifier.issn1016-8478-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/7802-
dc.description.abstractThe hepatitis B virus x protein (HBX) is expressed in HBV-infected 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 (1)H-(15)N HSQC NMR spectrum exhibits fewer number of resonances than expected, suggesting that Tr-HBX is a hybrid type IUP where its folded C-terminal 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.language.isoen-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHCircular Dichroism/methods-
dc.subject.MESHHepatitis B virus/genetics/*metabolism-
dc.subject.MESHMutagenesis, Site-Directed-
dc.subject.MESHNuclear Magnetic Resonance, Biomolecular-
dc.subject.MESHProtein Structure, Secondary-
dc.subject.MESHProtein Unfolding-
dc.subject.MESHTrans-Activators/*chemistry/genetics/isolation & purification/*metabolism-
dc.titleStructural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus-
dc.typeArticle-
dc.identifier.pmid22820921-
dc.identifier.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887815/-
dc.contributor.affiliatedAuthor조, 혜성-
dc.type.localJournal Papers-
dc.identifier.doi10.1007/s10059-012-0060-z-
dc.citation.titleMolecules and cells-
dc.citation.volume34-
dc.citation.number2-
dc.citation.date2012-
dc.citation.startPage165-
dc.citation.endPage169-
dc.identifier.bibliographicCitationMolecules and cells, 34(2):165-169, 2012-
dc.identifier.eissn0219-1032-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
Files in This Item:
fulltext not available.txtDownload

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse