The crystal structure of the human hepatitis B virus capsid.
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.
Wynne
S A
SA
Medical Research Council, Laboratory of Molecular Biology, Cambridge, United Kingdom.
Crowther
R A
RA
Leslie
A G
AG
D000595:Amino Acid Sequence; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000378:metabolism; D019281:Dimerization; D004220:Disulfides / Q000378:metabolism; D004583:Electrons; D000939:Epitopes / Q000737:chemistry; D006515:Hepatitis B virus / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017384:Sequence Deletion
D004220:Disulfides; D000939:Epitopes; D010446:Peptide Fragments; D003545:Cysteine