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PDBsum entry 5vcn
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Immune system
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PDB id
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5vcn
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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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PDB id:
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Immune system
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Title:
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The crystal structure of der p 1 allergen complexed with fab fragment of mab 5h8
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Structure:
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Peptidase 1. Chain: a, b. Synonym: allergen der p i, major mite fecal allergen der p 1. Light chain of fab fragment of mab 5h8. Chain: c, e. Engineered: yes. Heavy chain of fab fragment of mab 5h8. Chain: d, f. Engineered: yes
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Source:
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Dermatophagoides pteronyssinus. European house dust mite. Organism_taxid: 6956. Mus musculus. Organism_taxid: 10090. Expressed in: mus musculus. Expression_system_taxid: 10090. Expression_system_cell_line: hybridoma. Expression_system_cell_line: hybridoma
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Resolution:
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3.00Å
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R-factor:
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0.221
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R-free:
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0.265
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Authors:
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T.Osinski,K.A.Majorek,A.Pomes,L.R.Offermann,S.Osinski,J.Glesner, L.D.Vailes,M.D.Chapman,W.Minor,M.Chruszcz
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Key ref:
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T.Osinski
et al.
(2015).
Structural Analysis of Der p 1-Antibody Complexes and Comparison with Complexes of Proteins or Peptides with Monoclonal Antibodies.
J Immunol,
195,
307-316.
PubMed id:
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Date:
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31-Mar-17
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Release date:
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26-Apr-17
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Supersedes:
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PROCHECK
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Headers
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References
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P08176
(PEPT1_DERPT) -
Peptidase 1 from Dermatophagoides pteronyssinus
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Seq:
Struc:
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320 a.a.
222 a.a.*
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J Immunol
195:307-316
(2015)
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PubMed id:
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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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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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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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Links
