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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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PDB id:
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Complex (hemagglutinin/immunoglobulin)
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Title:
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Influenza virus hemagglutinin complexed with a neutralizing antibody
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Structure:
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Immunoglobulin (igg1, lambda). Chain: a. Fragment: fab fragment. Immunoglobulin (igg1, lambda). Chain: b. Fragment: fab fragment. Hemagglutinin. Chain: c. Fragment: proteolytic fragment "ha top" containing ha1 residues 28 -
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Strain: balb/c. Cell: hybridoma. Strain: balb-c. Influenza a virus (a/x-31(h3n2)). Organism_taxid: 132504. Strain: x31.
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Biol. unit:
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Homo-Trimer (from PDB file)
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Resolution:
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3.25Å
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R-factor:
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0.198
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R-free:
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0.249
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Authors:
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T.Bizebard,D.Fleury,B.Gigant,S.A.Wharton,J.J.Skehel,M.Knossow
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Key ref:
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D.Fleury
et al.
(1998).
Antigen distortion allows influenza virus to escape neutralization.
Nat Struct Biol,
5,
119-123.
PubMed id:
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Date:
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22-Dec-97
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Release date:
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29-Apr-98
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Supersedes:
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Nat Struct Biol
5:119-123
(1998)
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PubMed id:
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Antigen distortion allows influenza virus to escape neutralization.
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D.Fleury,
S.A.Wharton,
J.J.Skehel,
M.Knossow,
T.Bizebard.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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P.L.Kastritis,
I.H.Moal,
H.Hwang,
Z.Weng,
P.A.Bates,
A.M.Bonvin,
and
J.Janin
(2011).
A structure-based benchmark for protein-protein binding affinity.
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Protein Sci,
20,
482-491.
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T.Han,
and
W.A.Marasco
(2011).
Structural basis of influenza virus neutralization.
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Ann N Y Acad Sci,
1217,
178-190.
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A.Malik,
A.Firoz,
V.Jha,
E.Sunderasan,
and
S.Ahmad
(2010).
Modeling the three-dimensional structures of an unbound single-chain variable fragment (scFv) and its hypothetical complex with a Corynespora cassiicola toxin, cassiicolin.
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J Mol Model,
16,
1883-1893.
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A.Yokota,
K.Tsumoto,
M.Shiroishi,
T.Nakanishi,
H.Kondo,
and
I.Kumagai
(2010).
Contribution of asparagine residues to the stabilization of a proteinaceous antigen-antibody complex, HyHEL-10-hen egg white lysozyme.
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J Biol Chem,
285,
7686-7696.
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PDB codes:
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W.D.Lees,
D.S.Moss,
and
A.J.Shepherd
(2010).
A computational analysis of the antigenic properties of haemagglutinin in influenza A H3N2.
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Bioinformatics,
26,
1403-1408.
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Y.Sun,
Y.Shi,
W.Zhang,
Q.Li,
D.Liu,
C.Vavricka,
J.Yan,
and
G.F.Gao
(2010).
In silico characterization of the functional and structural modules of the hemagglutinin protein from the swine-origin influenza virus A (H1N1)-2009.
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Sci China Life Sci,
53,
633-642.
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D.C.Ekiert,
G.Bhabha,
M.A.Elsliger,
R.H.Friesen,
M.Jongeneelen,
M.Throsby,
J.Goudsmit,
and
I.A.Wilson
(2009).
Antibody recognition of a highly conserved influenza virus epitope.
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Science,
324,
246-251.
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PDB codes:
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B.D.Silverman
(2007).
Using molecular principal axes for structural comparison: determining the tertiary changes of a FAB antibody domain induced by antigenic binding.
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BMC Struct Biol,
7,
77.
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M.Shiroishi,
K.Tsumoto,
Y.Tanaka,
A.Yokota,
T.Nakanishi,
H.Kondo,
and
I.Kumagai
(2007).
Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL.
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J Biol Chem,
282,
6783-6791.
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PDB codes:
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B.J.Hanson,
A.C.Boon,
A.P.Lim,
A.Webb,
E.E.Ooi,
and
R.J.Webby
(2006).
Passive immunoprophylaxis and therapy with humanized monoclonal antibody specific for influenza A H5 hemagglutinin in mice.
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Respir Res,
7,
126.
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M.Knossow,
and
J.J.Skehel
(2006).
Variation and infectivity neutralization in influenza.
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Immunology,
119,
1-7.
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J.Yan,
W.Wen,
W.Xu,
J.F.Long,
M.E.Adams,
S.C.Froehner,
and
M.Zhang
(2005).
Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin.
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EMBO J,
24,
3985-3995.
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PDB codes:
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K.Nakajima,
E.Nobusawa,
A.Nagy,
and
S.Nakajima
(2005).
Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution.
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J Virol,
79,
6472-6477.
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I.Kumagai,
Y.Nishimiya,
H.Kondo,
and
K.Tsumoto
(2003).
Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10.
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J Biol Chem,
278,
24929-24936.
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PDB codes:
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I.B.Rasmussen,
E.Lunde,
T.E.Michaelsen,
B.Bogen,
and
I.Sandlie
(2001).
The principle of delivery of T cell epitopes to antigen-presenting cells applied to peptides from influenza virus, ovalbumin, and hen egg lysozyme: implications for peptide vaccination.
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Proc Natl Acad Sci U S A,
98,
10296-10301.
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D.Fleury,
R.S.Daniels,
J.J.Skehel,
M.Knossow,
and
T.Bizebard
(2000).
Structural evidence for recognition of a single epitope by two distinct antibodies.
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Proteins,
40,
572-578.
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PDB code:
|
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J.J.Skehel,
and
D.C.Wiley
(2000).
Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.
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Annu Rev Biochem,
69,
531-569.
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|
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B.Selisko,
A.F.Licea,
B.Becerril,
F.Zamudio,
L.D.Possani,
and
E.Horjales
(1999).
Antibody BCF2 against scorpion toxin Cn2 from Centuroides noxius Hoffmann: primary structure and three-dimensional model as free Fv fragment and complexed with its antigen.
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Proteins,
37,
130-143.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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');
}
}
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