3RVU

Structure of 4C1 Fab in C2221 space group

Summary for 3RVU

• Entry DOI: 10.2210/pdb3rvu/pdb
• Related: 3RVT 3RVV 3RVW 3RVX
• Descriptor: 4C1 Fab - light chain, 4C1 Fab - heavy chain (3 entities in total)
• Functional Keywords: igg, antibody, der f 1, der p 1, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 2
• Total formula weight: 51614.92

Authors

Chruszcz, M.,Vailes, L.D.,Chapman, M.D.,Pomes, A.,Minor, W. (deposition date: 2011-05-06, release date: 2012-01-11, Last modification date: 2024-11-06)

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., 287:7388-7398, 2012

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: 22210776
DOI: 10.1074/jbc.M111.311159

Experimental method

X-RAY DIFFRACTION (2.5 Å)