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PDBsum entry 4pp1
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Immune system
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PDB id
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4pp1
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Contents |
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222 a.a.
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210 a.a.
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213 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural analysis of der p 1-Antibody complexes and comparison with complexes of proteins or peptides with monoclonal antibodies.
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Authors
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T.Osinski,
A.Pomés,
K.A.Majorek,
J.Glesner,
L.R.Offermann,
L.D.Vailes,
M.D.Chapman,
W.Minor,
M.Chruszcz.
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Ref.
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J Immunol, 2015,
195,
307-316.
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PubMed id
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Abstract
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Der p 1 is a major allergen from the house dust mite, Dermatophagoides
pteronyssinus, that belongs to the papain-like cysteine protease family. To
investigate the antigenic determinants of Der p 1, we determined two crystal
structures of Der p 1 in complex with the Fab fragments of mAbs 5H8 or 10B9.
Epitopes for these two Der p 1-specific Abs are located in different,
nonoverlapping parts of the Der p 1 molecule. Nevertheless, surface area and
identity of the amino acid residues involved in hydrogen bonds between allergen
and Ab are similar. The epitope for mAb 10B9 only showed a partial overlap with
the previously reported epitope for mAb 4C1, a cross-reactive mAb that binds Der
p 1 and its homolog Der f 1 from Dermatophagoides farinae. Upon binding to Der p
1, the Fab fragment of mAb 10B9 was found to form a very rare α helix in its
third CDR of the H chain. To provide an overview of the surface properties of
the interfaces formed by the complexes of Der p 1-10B9 and Der p 1-5H8, along
with the complexes of 4C1 with Der p 1 and Der f 1, a broad analysis of the
surfaces and hydrogen bonds of all complexes of Fab-protein or Fab-peptide was
performed. This work provides detailed insight into the cross-reactive and
specific allergen-Ab interactions in group 1 mite allergens. The surface data of
Fab-protein and Fab-peptide interfaces can be used in the design of
conformational epitopes with reduced Ab binding for immunotherapy.
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