The crystal structure of the human hepatitis B virus capsid

Mol Cell. 1999 Jun;3(6):771-80. doi: 10.1016/s1097-2765(01)80009-5.


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.

MeSH terms

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


  • Disulfides
  • Epitopes
  • Peptide Fragments
  • Cysteine

Associated data

  • PDB/1QGT