Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy

J. F. Conway, N. Cheng, A. Zlotnick, P. T. Wingfield, S. J. Stahl and A. C. Steven
Additional contact information
J. F. Conway: National Institutes of Health
N. Cheng: National Institutes of Health
A. Zlotnick: National Institutes of Health
P. T. Wingfield: National Institutes of Health
S. J. Stahl: National Institutes of Health
A. C. Steven: National Institutes of Health

Nature, 1997, vol. 386, issue 6620, 91-94

Abstract: Abstract Despite the development of vaccines, the hepatitis B virus remains a major cause of human liver disease1. The virion consists of a lipoprotein envelope surrounding an icosahedral capsid composed of dimers of a 183-residue protein, 'core antigen' (HBcAg)2. Knowledge of its structure is important for the design of antiviral drugs, but it has yet to be determined. Residues 150–183 are known to form a protamine-like domain required for packaging RNA, and residues 1–149 form the 'assembly domain' that polymerizes into capsids2 and, unusually for a capsid protein, is highly α-helical3. Density maps calculated from cryo-electron micrographs4–6 show that the assembly domain dimer is T-shaped: its stem constitutes the dimer interface and the tips of its arms make the polymerization contacts. By refining the procedures used to calculate the map, we have extended the resolution to 9 Å, revealing major elements of secondary structure. In particular, the stem, which protrudes as a spike on the capsid's outer surface, is a 4-helix bundle, formed by the pairing of α-helical hairpins from both subunits.

Date: 1997
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/386091a0 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:386:y:1997:i:6620:d:10.1038_386091a0

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/386091a0

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().