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PDBsum entry 1ken
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Viral protein/immune system
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PDB id
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1ken
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Contents |
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320 a.a.
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175 a.a.
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213 a.a.
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221 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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An antibody that prevents the hemagglutinin low ph fusogenic transition.
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Authors
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C.Barbey-Martin,
B.Gigant,
T.Bizebard,
L.J.Calder,
S.A.Wharton,
J.J.Skehel,
M.Knossow.
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Ref.
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Virology, 2002,
294,
70-74.
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PubMed id
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Abstract
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We have determined the structure of a complex of influenza hemagglutinin (HA)
with an antibody that binds simultaneously to the membrane-distal domains of two
HA monomers, effectively cross-linking them. The antibody prevents the low pH
structural transition of HA that is required for its membrane fusion activity,
providing evidence that a rearrangement of HA membrane-distal domains is an
essential component of the transition.
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Secondary reference #1
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Title
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A neutralizing antibody FAB-Influenza haemagglutinin complex with an unprecedented 2:1 stoichiometry: characterization and crystallization.
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Authors
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B.Gigant,
C.Barbey-Martin,
T.Bizebard,
D.Fleury,
R.Daniels,
J.J.Skehel,
M.Knossow.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
1067-1069.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 Fit of the X31 BHA-HC63 Fab equilibrium sedimentation
data. Equilibrium sedimentation data obtained at 4500 and 5200
rev min-1 were fitted to a monodisperse model. The open circles
represent the data from the 4500 rev min-1 run and the solid
line is the fit. The residuals representing the variation
between the experimental data and those generated by the fit are
also plotted (upper panel); the molecular weight deduced from
the fit is 306 kDa (standard deviation is 1 kDa). Theoretical
curves for absorbance versus radius based on the molecular
weights of the 1:1 and the 3:1 Fab-BHA complexes are also
plotted (lower panel). The data confirm the 2:1
Fab:(BHA trimer) stoichiometry observed in the structure.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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