5vph | pdb_00005vph

CRYSTAL STRUCTURE OF DER P 1 COMPLEXED WITH FAB 4C1

spinqualitylabelsall models 5vph, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vph is a 3 chain structure with sequence from Dermatophagoides pteronyssinus and Mus musculus. This structure supersedes the now removed PDB entry 3rvx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CA, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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