This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1qgt
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)== |
| + | <StructureSection load='1qgt' size='340' side='right' caption='[[1qgt]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1qgt]] is a 4 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QGT FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1qgt RCSB], [http://www.ebi.ac.uk/pdbsum/1qgt PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:10394365</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Virus coat protein|Virus coat protein]] | *[[Virus coat protein|Virus coat protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Hepatitis b virus]] | [[Category: Hepatitis b virus]] | ||
[[Category: Crowther, R A.]] | [[Category: Crowther, R A.]] | ||
Revision as of 20:09, 28 September 2014
HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)
| |||||||||||
