Structural highlights
Function
PEPT1_DERPT Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues.
Publication Abstract from PubMed
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.
Molecular determinants for antibody binding on group 1 house dust mite allergens.,Chruszcz M, Pomes A, Glesner J, Vailes LD, Osinski T, Porebski PJ, Majorek KA, Heymann PW, Platts-Mills TA, Minor W, Chapman MD J Biol Chem. 2012 Mar 2;287(10):7388-98. Epub 2011 Dec 30. PMID:22210776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chruszcz M, Pomes A, Glesner J, Vailes LD, Osinski T, Porebski PJ, Majorek KA, Heymann PW, Platts-Mills TA, Minor W, Chapman MD. Molecular determinants for antibody binding on group 1 house dust mite allergens. J Biol Chem. 2012 Mar 2;287(10):7388-98. Epub 2011 Dec 30. PMID:22210776 doi:10.1074/jbc.M111.311159
