Structural and Functional Characterization of Interaction between Hepatitis B Virus X Protein and the Proteasome Complex

Hepatitis B virus (HBV) has a unique fourth open reading frame coding for a 16.5-kDa protein known as hepatitis B virus X protein (HBX). The importance of HBX in the life cycle of HBV has been well established, but the underlying molecular function of HBX remains controversial. We previously identif...

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Veröffentlicht in:	The Journal of biological chemistry 2000-05, Vol.275 (20), p.15157-15165
Hauptverfasser:	Zhang, Zhensheng, Torii, Nobuyuki, Furusaka, Akihiro, Malayaman, Navara, Hu, Zongyi, Liang, T.Jake
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Animals AX protein Cloning, Molecular Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - metabolism Hepatitis B Antigens - chemistry Hepatitis B Antigens - metabolism Hepatitis B virus Hepatitis B virus - genetics Kinetics Macromolecular Substances Models, Molecular Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Open Reading Frames Proteasome Endopeptidase Complex proteasomes Protein Binding Protein Biosynthesis Protein Structure, Quaternary PSMA7 protein PSMC1 protein Rabbits Recombinant Proteins - chemistry Recombinant Proteins - metabolism Reticulocytes - metabolism Saccharomyces cerevisiae - genetics Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Viral Regulatory and Accessory Proteins
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