1QGT

HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)

Summary for 1QGT

• Entry DOI: 10.2210/pdb1qgt/pdb
• Descriptor: PROTEIN (HBV CAPSID PROTEIN) (1 entity in total)
• Functional Keywords: viral capsid protein, icosahedral virus, virus
• Biological source: Hepatitis B virus
• Total number of polymer chains: 4
• Total formula weight: 67465.13

Authors

Leslie, A.G.W.,Wynne, S.A.,Crowther, R.A. (deposition date: 1999-05-05, release date: 1999-06-25, Last modification date: 2024-10-09)

Primary citation

Wynne, S.A.,Crowther, R.A.,Leslie, A.G.
The crystal structure of the human hepatitis B virus capsid.
Mol.Cell, 3:771-780, 1999

PubMed 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.

PubMed: 10394365
DOI: 10.1016/S1097-2765(01)80009-5

Experimental method

X-RAY DIFFRACTION (3.3 Å)