3v6f: Difference between revisions
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[[ | ==Crystal Structure of an anti-HBV e-antigen monoclonal Fab fragment (e6), unbound== | ||
<StructureSection load='3v6f' size='340' side='right' caption='[[3v6f]], [[Resolution|resolution]] 2.52Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v6f]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V6F FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v6z|3v6z]]</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=3v6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v6f RCSB], [http://www.ebi.ac.uk/pdbsum/3v6f 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: 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: Antibody fab fragment]] | [[Category: Antibody fab fragment]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Immunoglobulin domain]] | [[Category: Immunoglobulin domain]] | ||
Revision as of 20:41, 9 December 2014
Crystal Structure of an anti-HBV e-antigen monoclonal Fab fragment (e6), unboundCrystal Structure of an anti-HBV e-antigen monoclonal Fab fragment (e6), unbound
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
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