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

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Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus
Si Hyung Lee; Eun Ji Cha; J E Lim; S H Kwon; Do Hyoung Kim; H Cho; Kyou Hoon Han
Bibliographic Citation
Molecules and Cells, vol. 34, no. 2, pp. 165-169
Publication Year
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.
Circular dichroism (CD) spectropolarimetryHepatitis B virus-X (HBX)Intrinsically unstructured/unfolded protein (IUP)Nuclear magnetic resonance (NMR) spectroscopyPromiscuityTruncated mini-HBX (Tr-HBX)
Korea Soc-Assoc-Inst
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Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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