Summary for 5VCN
| Entry DOI | 10.2210/pdb5vcn/pdb |
| Related | 3RVV 3RVW 3RVX 4POZ 4PP2 5VCO |
| Descriptor | PEPTIDASE 1, LIGHT CHAIN OF FAB FRAGMENT OF MAB 5H8, HEAVY CHAIN OF FAB FRAGMENT OF MAB 5H8, ... (8 entities in total) |
| Functional Keywords | allergen, antibody, immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 6 |
| Total formula weight | 153333.09 |
| 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: 2017-03-31, release date: 2017-04-26, Last modification date: 2024-11-20) |
| 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 Cited by 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: 26026055DOI: 10.4049/jimmunol.1402199 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
