Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein.
Hepatitis C virus core protein plays an important role in the assembly and packaging of the viral genome. We have studied the structure of the N-terminal half of the core protein (C82) which was shown to be sufficient for the formation of nucleocapsid-like particle (NLP) in vitro and in yeast. Structural bioinformatics analysis of C82 suggests that it is mostly unstructured. Circular dichroism and structural NMR data indicate that C82 lacks secondary structure. Moreover, NMR relaxation data shows that C82 is highly disordered. These results indicate that the N-terminal half of the HCV core protein belongs to the growing family of intrinsically unstructured proteins (IUP). This explains the tendency of the hepatitis C virus core protein to interact with several host proteins, a well-documented characteristic of IUPs.
Duvignaud
Jean-Baptiste
JB
CREFSIP and Department of Biochemistry and Microbiology, Université Laval, 1030 Avenue de la Médecine, Local 3255, Québec, QC, Canada G1V 0A6.
Savard
Christian
C
Fromentin
Rémi
R
Majeau
Nathalie
N
Leclerc
Denis
D
Gagné
Stéphane M
SM
D000595:Amino Acid Sequence; D016174:Hepacivirus / Q000378:metabolism*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D020539:Sequence Analysis, Protein; D014758:Viral Core Proteins / Q000737:chemistry* / Q000648:ultrastructure
D014758:Viral Core Proteins; C069130:nucleocapsid protein, Hepatitis C virus