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1qgt

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgt OCA], [http://www.ebi.ac.uk/pdbsum/1qgt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgt RCSB]</span>
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[[Category: viral capsid protein]]
[[Category: viral capsid protein]]
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Revision as of 20:13, 30 March 2008

Image:1qgt.gif


PDB ID 1qgt

Drag the structure with the mouse to rotate
, resolution 3.3Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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