1A92

OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN

Summary for 1A92

• Entry DOI: 10.2210/pdb1a92/pdb
• Descriptor: DELTA ANTIGEN (2 entities in total)
• Functional Keywords: leucine zipper, coiled-coil, oligomerization, hepatitis delta, hdv
• Biological source: Hepatitis delta virus
• Total number of polymer chains: 4
• Total formula weight: 24024.20

Authors

Zuccola, H.J.,Hogle, J.M. (deposition date: 1998-04-15, release date: 1999-06-08, Last modification date: 2024-02-07)

Primary citation

Zuccola, H.J.,Rozzelle, J.E.,Lemon, S.M.,Erickson, B.W.,Hogle, J.M.
Structural basis of the oligomerization of hepatitis delta antigen.
Structure, 6:821-830, 1998

PubMed Abstract: The hepatitis D virus (HDV) is a small satellite virus of hepatitis B virus (HBV). Coinfection with HBV and HDV causes severe liver disease in humans. The small 195 amino-acid form of the hepatitis delta antigen (HDAg) functions as a trans activator of HDV replication. A larger form of the protein containing a 19 amino acid C-terminal extension inhibits viral replication. Both of these functions are mediated in part by a stretch of amino acids predicted to form a coiled coil (residues 13-48) that is common to both forms. It is believed that HDAg forms dimers and higher ordered structures through this coiled-coil region.

PubMed: 9687364
DOI: 10.1016/S0969-2126(98)00084-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)