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...

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Bibliographic Details
Published in:Molecular cell 1999-06, Vol.3 (6), p.771-780
Main Authors: Wynne, S A, Crowther, R A, Leslie, A G
Format: Article
Language:English
Subjects:
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
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
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Summary: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.
ISSN:1097-2765
1097-4164
1097-4164
DOI:10.1016/s1097-2765(01)80009-5