1by0
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N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN
OverviewOverview
Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus, (HBV) which provides the surface antigen for the viral coat. The RNA, genome of HDV encodes two proteins: the small delta antigen and the large, delta antigen. The two proteins resemble each other except for the, presence of an additional 19 amino acids at the C terminus of the latter, species. We have found that the N-terminal leucine-repeat region of, hepatitis delta antigen (HDAg) binds to the autolytic domain of HDV, genomic RNA and attenuates its autolytic activity. A 27-residue, polypeptide corresponding to residues 24-50 of HDAg, designated, dAg(24-50), was synthesized, and its solution structure was found to be an, alpha-helix by circular dichroism and (1)H-nuclear magnetic resonance, (NMR) techniques. Binding affinity of dAg(24-50) with HDV genomic RNA was, found to increase with its alpha-helical content, and it was further, confirmed by modifying its N- and C-terminal groups. Furthermore, the, absence of RNA binding activity in the mutant peptides, dAgM(24-50am) and, dAgM(Ac24-50am), in which Lys38, Lys39, and Lys40 were changed to Glu, indicates a possible involvement of these residues in their binding, activity. Structural knowledge of the N-terminal leucine-repeat region of, HDAg thus provides a molecular basis for the understanding of its role in, the interaction with RNA. Proteins 1999;37:121-129.
About this StructureAbout this Structure
1BY0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure and RNA-binding activity of the N-terminal leucine-repeat region of hepatitis delta antigen., Lin IJ, Lou YC, Pai MT, Wu HN, Cheng JW, Proteins. 1999 Oct 1;37(1):121-9. PMID:10451556
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