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1qgt
From Proteopedia
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[[Image:1qgt.gif|left|200px]] | [[Image:1qgt.gif|left|200px]] | ||
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'''HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)''' | '''HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)''' | ||
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[[Category: Leslie, A G.W.]] | [[Category: Leslie, A G.W.]] | ||
[[Category: Wynne, S A.]] | [[Category: Wynne, S A.]] | ||
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| - | [[Category: | + | [[Category: Viral capsid protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:15, 3 May 2008
HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)
Overview
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.
About this Structure
1QGT is a Single protein structure of sequence from Hepatitis b virus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the human hepatitis B virus capsid., Wynne SA, Crowther RA, Leslie AG, Mol Cell. 1999 Jun;3(6):771-80. PMID:10394365 Page seeded by OCA on Sat May 3 06:15:09 2008
