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PDBsum entry 2vir
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Complex (hemagglutinin/immunoglobulin)
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PDB id
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2vir
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Contents |
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210 a.a.
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221 a.a.
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267 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Antigen distortion allows influenza virus to escape neutralization.
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Authors
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D.Fleury,
S.A.Wharton,
J.J.Skehel,
M.Knossow,
T.Bizebard.
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Ref.
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Nat Struct Biol, 1998,
5,
119-123.
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PubMed id
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Abstract
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The structure of the hemagglutinin (HA) of a mutant influenza virus that escapes
neutralization by a monoclonal antibody shows that the mutation causes changes
in HA structure which avoid an energetically less favorable conformation.
However, the structure of the mutant HA.Fab complex indicates that the antibody
binds selectively to mutant HA in a wild type-like distorted conformation. The
association of an antibody with a less favored HA conformation represents an
alternative to previously described mechanisms of escape from neutralization by
antibodies.
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Secondary reference #1
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Title
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Structure of influenza virus haemagglutinin complexed with a neutralizing antibody.
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Authors
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T.Bizebard,
B.Gigant,
P.Rigolet,
B.Rasmussen,
O.Diat,
P.Bösecke,
S.A.Wharton,
J.J.Skehel,
M.Knossow.
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Ref.
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Nature, 1995,
376,
92-94.
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PubMed id
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Secondary reference #2
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Title
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Refined three-Dimensional structure of the FAB fragment of a murine iggl,Lambda antibody.
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Authors
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T.Bizebard,
R.Daniels,
R.Kahn,
B.Golinelli-Pimpaneau,
J.J.Skehel,
M.Knossow.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1994,
50,
768-777.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Primary sequence of HCI. (a) Lightchan sequence. (b) Partial
heavychin sequnce. CDRs are underlined.
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Figure 3.
Fig. 3. Diagrams of a 217o Fc electrondensity map of ab fragment
HC19 showing (a) CDR L2; the map is contoured at the 2 r.m.s.d.
leve. (b) CDR L3; the map is contoured at the 1.5 r.m.s.d, level.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #3
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Title
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 a resolution.
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Authors
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I.A.Wilson,
J.J.Skehel,
D.C.Wiley.
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Ref.
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Nature, 1981,
289,
366-373.
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PubMed id
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