The crystal structure of the human hepatitis B virus capsid. |
| |
Authors: | S A Wynne R A Crowther A G Leslie |
| |
Affiliation: | Medical Research Council, Laboratory of Molecular Biology, Cambridge, United Kingdom. |
| |
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. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |