1BY0

N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN

Summary for 1BY0

• Entry DOI: 10.2210/pdb1by0/pdb
• Descriptor: PROTEIN (HEPATITIS DELTA ANTIGEN) (1 entity in total)
• Functional Keywords: hepatitis delta antigen, helix, solution structure, rna binding, rna binding protein
• Total number of polymer chains: 1
• Total formula weight: 3475.15

Authors

Cheng, J.W.,Lin, I.J.,Lou, Y.C. (deposition date: 1998-10-22, release date: 1999-12-29, Last modification date: 2023-12-27)

Primary citation

Lin, I.J.,Lou, Y.C.,Pai, M.T.,Wu, H.N.,Cheng, J.W.
Solution structure and RNA-binding activity of the N-terminal leucine-repeat region of hepatitis delta antigen
Proteins, 37:121-129, 1999

PubMed Abstract: 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.

PubMed: 10451556
DOI: 10.1002/(SICI)1097-0134(19991001)37:1<121::AID-PROT12>3.3.CO;2-K

Experimental method

SOLUTION NMR