4POZ

Fab fragment of Der p 1 specific antibody 10B9

Summary for 4POZ

• Entry DOI: 10.2210/pdb4poz/pdb
• Related: 3RVV 3RVW 3RVX 4POZ 4PP1
• Descriptor: light chain of Fab fragment of 10B9 antibody, heavy chain of Fab fragment of 10B9 antibody (3 entities in total)
• Functional Keywords: antibody, allergy, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 2
• Total formula weight: 47415.66

Authors

Osinski, T.,Majorek, K.A.,Pomes, A.,Offermann, L.R.,Osinski, S.,Glesner, J.,Vailes, L.D.,Chapman, M.D.,Minor, W.,Chruszcz, M. (deposition date: 2014-02-26, release date: 2015-04-08, Last modification date: 2024-11-06)

Primary citation

Osinski, T.,Pomes, A.,Majorek, K.A.,Glesner, J.,Offermann, L.R.,Vailes, L.D.,Chapman, M.D.,Minor, W.,Chruszcz, M.
Structural Analysis of Der p 1-Antibody Complexes and Comparison with Complexes of Proteins or Peptides with Monoclonal Antibodies.
J. Immunol., 195:307-316, 2015

PubMed Abstract: 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.

PubMed: 26026055
DOI: 10.4049/jimmunol.1402199

Experimental method

X-RAY DIFFRACTION (1.75 Å)