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1qgt
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:21 2008'' |
Revision as of 20:13, 30 March 2008
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| , resolution 3.3Å | |||||||
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| 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
Page seeded by OCA on Sun Mar 30 23:13:21 2008
