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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

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      Abstract

      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.

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      10394365

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