3v6z: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crystal Structure of Hepatitis B Virus e-antigen== | ||
<StructureSection load='3v6z' size='340' side='right' caption='[[3v6z]], [[Resolution|resolution]] 3.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v6z]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_b_virus Hepatitis b virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V6Z FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v6f|3v6f]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">preC/C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10407 Hepatitis B virus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v6z RCSB], [http://www.ebi.ac.uk/pdbsum/3v6z PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chronic hepatitis B virus (HBV) infection afflicts millions worldwide with cirrhosis and liver cancer. HBV e-antigen (HBeAg), a clinical marker for disease severity, is a nonparticulate variant of the protein (core antigen, HBcAg) that forms the building-blocks of capsids. HBeAg is not required for virion production, but is implicated in establishing immune tolerance and chronic infection. Here, we report the crystal structure of HBeAg, which clarifies how the short N-terminal propeptide of HBeAg induces a radically altered mode of dimerization relative to HBcAg ( approximately 140 degrees rotation), locked into place through formation of intramolecular disulfide bridges. This structural switch precludes capsid assembly and engenders a distinct antigenic repertoire, explaining why the two antigens are cross-reactive at the T cell level (through sequence identity) but not at the B cell level (through conformation). The structure offers insight into how HBeAg may establish immune tolerance for HBcAg while evading its robust immunogenicity. | |||
Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.,Dimattia MA, Watts NR, Stahl SJ, Grimes JM, Steven AC, Stuart DI, Wingfield PT Structure. 2013 Jan 8;21(1):133-42. doi: 10.1016/j.str.2012.10.017. Epub 2012 Dec, 6. PMID:23219881<ref>PMID:23219881</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Hepatitis b virus]] | [[Category: Hepatitis b virus]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Dimattia, M A | [[Category: Dimattia, M A]] | ||
[[Category: Grimes, J M | [[Category: Grimes, J M]] | ||
[[Category: Stahl, S J | [[Category: Stahl, S J]] | ||
[[Category: Steven, A C | [[Category: Steven, A C]] | ||
[[Category: Stuart, D I | [[Category: Stuart, D I]] | ||
[[Category: Watts, N R | [[Category: Watts, N R]] | ||
[[Category: Wingfield, P T | [[Category: Wingfield, P T]] | ||
[[Category: Dimer inversion]] | [[Category: Dimer inversion]] | ||
[[Category: Four-helix bundle]] | [[Category: Four-helix bundle]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
Revision as of 19:44, 9 December 2014
Crystal Structure of Hepatitis B Virus e-antigenCrystal Structure of Hepatitis B Virus e-antigen
Structural highlights
Publication Abstract from PubMedChronic hepatitis B virus (HBV) infection afflicts millions worldwide with cirrhosis and liver cancer. HBV e-antigen (HBeAg), a clinical marker for disease severity, is a nonparticulate variant of the protein (core antigen, HBcAg) that forms the building-blocks of capsids. HBeAg is not required for virion production, but is implicated in establishing immune tolerance and chronic infection. Here, we report the crystal structure of HBeAg, which clarifies how the short N-terminal propeptide of HBeAg induces a radically altered mode of dimerization relative to HBcAg ( approximately 140 degrees rotation), locked into place through formation of intramolecular disulfide bridges. This structural switch precludes capsid assembly and engenders a distinct antigenic repertoire, explaining why the two antigens are cross-reactive at the T cell level (through sequence identity) but not at the B cell level (through conformation). The structure offers insight into how HBeAg may establish immune tolerance for HBcAg while evading its robust immunogenicity. Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.,Dimattia MA, Watts NR, Stahl SJ, Grimes JM, Steven AC, Stuart DI, Wingfield PT Structure. 2013 Jan 8;21(1):133-42. doi: 10.1016/j.str.2012.10.017. Epub 2012 Dec, 6. PMID:23219881[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||