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

Authors
Lee, SH; Cha, EJ; Lim, JE; Kwon, SH; Kim, DH; Cho, H; Han, KH
Citation
Molecules and cells, 34(2):165-169, 2012
Journal Title
Molecules and cells
ISSN
1016-84780219-1032
Abstract
The 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.
MeSH terms
Amino Acid SequenceCircular Dichroism/methodsHepatitis B virus/genetics/*metabolismMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProtein UnfoldingTrans-Activators/*chemistry/genetics/isolation & purification/*metabolism
DOI
10.1007/s10059-012-0060-z
PMID
22820921
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
AJOU Authors
조, 혜성
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