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Title 

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

Authors 

Si Hyung LeeEun Ji ChaJ E LimS H KwonDo Hyoung KimH ChoKyou Hoon Han

Publisher 

Springer Verlag (Germany)

Issue Date 

2012

Citation 

Molecules and Cells, vol. 34, no. 2, pp. 165-169

Keywords 

Circular dichroism (CD) spectropolarimetryHepatitis B virus-X (HBX)Intrinsically unstructured/unfolded protein (IUP)Nuclear magnetic resonance (NMR) spectroscopyPromiscuityTruncated mini-HBX (Tr-HBX) --------------------------------------------------------------------------------

Abstract 

The 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.

ISSN 

1016-8478

Link 

http://dx.doi.org/10.1007/s10059-012-0060-z

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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