• Record: found
  • Abstract: found
  • Article: not found

The crystal structure of the human hepatitis B virus capsid.

Molecular Cell

Amino Acid Sequence, Binding Sites, Capsid, chemistry, genetics, metabolism, Conserved Sequence, Crystallization, Crystallography, X-Ray, Cysteine, Dimerization, Disulfides, Electrons, Epitopes, Hepatitis B virus, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Sequence Deletion, Protein Binding, Protein Folding, Protein Structure, Secondary

Read this article at

      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


      Hepatitis B is a small enveloped DNA virus that poses a major hazard to human health. The crystal structure of the T = 4 capsid has been solved at 3.3 A resolution, revealing a largely helical protein fold that is unusual for icosahedral viruses. The monomer fold is stabilized by a hydrophobic core that is highly conserved among human viral variants. Association of two amphipathic alpha-helical hairpins results in formation of a dimer with a four-helix bundle as the major central feature. The capsid is assembled from dimers via interactions involving a highly conserved region near the C terminus of the truncated protein used for crystallization. The major immunodominant region lies at the tips of the alpha-helical hairpins that form spikes on the capsid surface.

      Related collections

      Author and article information



      Comment on this article