Summary for 5VPL
| Entry DOI | 10.2210/pdb5vpl/pdb |
| Related | 5VPG 5VPH 5VPK |
| Descriptor | Der f 1 variant, 4C1 - LIGHT CHAIN, 4C1 - HEAVY CHAIN, ... (7 entities in total) |
| Functional Keywords | complex between an allergen and fab fragment of 4c1 antibody, hydrolase-immune system complex, hydrolase/immune system |
| Biological source | Mus musculus (MOUSE) More |
| Total number of polymer chains | 3 |
| Total formula weight | 77295.45 |
| Authors | Chruszcz, M.,Vailes, L.D.,Chapman, M.D.,Pomes, A.,Minor, W. (deposition date: 2017-05-05, release date: 2017-05-24, Last modification date: 2023-10-04) |
| Primary citation | Chruszcz, M.,Pomes, A.,Glesner, J.,Vailes, L.D.,Osinski, T.,Porebski, P.J.,Majorek, K.A.,Heymann, P.W.,Platts-Mills, T.A.,Minor, W.,Chapman, M.D. Molecular Determinants For Antibody Binding On Group 1 House Dust Mite Allergens. J.Biol.Chem., 287:7388-, 2012 Cited by PubMed Abstract: House dust mites produce potent allergens, Der p 1 and Der f 1, that cause allergic sensitization and asthma. Der p 1 and Der f 1 are cysteine proteases that elicit IgE responses in 80% of mite-allergic subjects and have proinflammatory properties. Their antigenic structure is unknown. Here, we present crystal structures of natural Der p 1 and Der f 1 in complex with a monoclonal antibody, 4C1, which binds to a unique cross-reactive epitope on both allergens associated with IgE recognition. The 4C1 epitope is formed by almost identical amino acid sequences and contact residues. Mutations of the contact residues abrogate mAb 4C1 binding and reduce IgE antibody binding. These surface-exposed residues are molecular targets that can be exploited for development of recombinant allergen vaccines. PubMed: 22210776DOI: 10.1074/JBC.M111.311159 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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