ArticleJournal of biomolecular NMR1998
Local helix content and RNA-binding activity of the N-terminal leucine-repeat region of hepatitis delta antigen.
Article in Journal of biomolecular NMR, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Article
- Molecular evolution of the hepatitis delta virus antigen gene: recombination or positive selection?Journal of molecular evolution · 2004Article
- Interaction and replication activation of genotype I and II hepatitis delta antigens.Journal of virology · 2004Article
- Hepatitis delta virus minimal substrates competent for editing by ADAR1 and ADAR2.Journal of virology · 2001Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus (HBV) which provides the surface antigen for the viral coat. Our results show that the N-terminal leucine-repeat region of hepatitis delta antigen (HDAg), encompassing residues 24-50, binds to the autolytic domain of HDV genomic RNA and attenuates its autolytic activity. The solution conformation of a synthetic peptide corresponding to residues 24-50 of HDAg as determined by two-dimensional 1H NMR and circular dichroism techniques is found to be an alpha-helix. The local helix content of this peptide was analyzed by NOEs and coupling constants. Mutagenesis studies indicate that Lys38, Lys39, and Lys40 within this alpha-helical peptide may be directly involved in RNA binding. A structural knowledge of the N-terminal leucine-repeat region of HDAg thus provides a molecular basis for understanding its role in the interaction with RNA.
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