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)''' | + | {{Structure |
| + | |PDB= 1qgt |SIZE=350|CAPTION= <scene name='initialview01'>1qgt</scene>, resolution 3.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QGT is a [ | + | 1QGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_b_virus Hepatitis b virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10394365 10394365] |
[[Category: Hepatitis b virus]] | [[Category: Hepatitis b virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral capsid protein]] | [[Category: viral capsid protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:13 2008'' |
Revision as of 11:37, 20 March 2008
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| , resolution 3.3Å | |||||||
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| 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 Thu Mar 20 13:37:13 2008
