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PDBsum entry 1fbi
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Complex (antibody/antigen)
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PDB id
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1fbi
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Contents |
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214 a.a.
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221 a.a.
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129 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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Crystal structure of a cross-Reaction complex between FAB f9.13.7 and guinea fowl lysozyme.
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Authors
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J.Lescar,
M.Pellegrini,
H.Souchon,
D.Tello,
R.J.Poljak,
N.Peterson,
M.Greene,
P.M.Alzari.
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Ref.
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J Biol Chem, 1995,
270,
18067-18076.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
91%.
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Abstract
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The crystal structure of the complex between the cross-reacting antigen Guinea
fowl lysozyme and the Fab from monoclonal antibody F9.13.7, raised against hen
egg lysozyme, has been determined by x-ray diffraction to 3-A resolution. The
antibody interacts with exposed residues of an alpha-helix and surrounding loops
adjacent to the lysozyme active site cleft. The epitope of lysozyme bound by
antibody F9.13.7 overlaps almost completely with that bound by antibody HyHEL10;
the same 12 residues of the antigen interact with the two antibodies. The
antibodies, however, have different combining sites with no sequence homology at
any of their complementarity-determining regions and show a dissimilar pattern
of cross-reactivity with heterologous antigens. Side chain mobility of epitope
residues contributes to confer steric and electrostatic complementarity to
differently shaped combining sites, allowing functional mimicry to occur. The
capacity of two antibodies that have different fine specificities to bind the
same area of the antigen emphasizes the operational character of the definition
of an antigenic determinant. This example demonstrates that degenerate binding
of the same structural motif does not require the existence of sequence homology
or other chemical similarities between the different binding sites.
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Secondary reference #1
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Title
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Crystal structures of pheasant and guinea fowl egg-White lysozymes.
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Authors
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J.Lescar,
H.Souchon,
P.M.Alzari.
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Ref.
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Protein Sci, 1994,
3,
788-798.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. Electron density 2F0 - F,) maps contoured at 1.00.
oop 100-14 of PHL, (A)and PHLb (B), conserved inter-
nal olvent molecules in PHL, (C) and GEL D), stack-
ing interactions of 62 n GEL (E).
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Figure 6.
Fig. 6. Superposition of PHL, (blue)
andPHLb (red) showing thedifferent
conformations adopted by the N-terminal
Gly 0 residue. The Ccz atoms of 41
and of the side chains thatform ahydro-
en bond with the NH3-group are labeled.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the Protein Society
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Secondary reference #2
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Title
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Crystallization, Preliminary X-Ray diffraction study, And crystal packing of a complex between anti-Hen lysozyme antibody f9.13.7 and guinea-Fowl lysozyme.
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Authors
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J.Lescar,
M.M.Riottot,
H.Souchon,
V.Chitarra,
G.A.Bentley,
J.Navaza,
P.M.Alzari,
R.J.Poljak.
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Ref.
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Proteins, 1993,
15,
209-212.
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PubMed id
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