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PDBsum entry 3v6f
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Immune system
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PDB id
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3v6f
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PDB id:
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| Name: |
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Immune system
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Title:
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Crystal structure of an anti-hbv e-antigen monoclonal fab fragment (e6), unbound
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Structure:
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Fab e6 heavy chain. Chain: a, c, e, h. Fab e6 light chain. Chain: b, d, f, l
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Source:
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Mus musculus. Organism_taxid: 10090. Organism_taxid: 10090
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Resolution:
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2.52Å
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R-factor:
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0.181
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R-free:
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0.220
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Authors:
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M.A.Dimattia,N.R.Watts,S.J.Stahl,J.M.Grimes,A.C.Steven,D.I.Stuart, P.T.Wingfield
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Key ref:
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M.A.DiMattia
et al.
(2013).
Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.
Structure,
21,
133-142.
PubMed id:
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Date:
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19-Dec-11
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Release date:
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06-Feb-13
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PROCHECK
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Headers
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References
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Structure
21:133-142
(2013)
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PubMed id:
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Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.
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M.A.DiMattia,
N.R.Watts,
S.J.Stahl,
J.M.Grimes,
A.C.Steven,
D.I.Stuart,
P.T.Wingfield.
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ABSTRACT
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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 (∼140° 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.
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Links
