9nph

X-ray crystal structure of recombinant Can f 1 in complex with human IgE mAb 1J11 Fab

spinqualitylabelsall models 9nph, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9nph is a 3 chain structure with sequence from Canis lupus familiaris and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.592Å Ligands: EPE, NAG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALL1_CANLF Publication Abstract from PubMed Molecular analysis of interactions between IgE antibody and allergen allows the structural basis of IgE recognition to be defined. Human IgE (hIgE) epitopes of respiratory lipocalin allergens, including Can f 1, remain elusive due to a lack of IgE-allergen complexes. This study aims to map the structure of allergenic epitopes on Can f 1. The fragment antigen-binding (Fab) regions of Can f 1 specific human IgE monoclonal antibodies (hIgE mAb) were used to determine the structures of IgE epitopes. Epitope mutants were designed to target Can f 1 epitopes. Immunoassays and a human FcepsilonRIalpha transgenic mouse model of passive anaphylaxis in vivo were used to assess the functional activity of epitope mutants. Crystal structures of natural or recombinant Can f 1 complexed with two hIgE mAb 1J11 and 12F3 Fabs, respectively, were determined. The hIgE mAb bound to two partially overlapping epitopes and recognized two different Can f 1 conformations. The hIgE mAb 12F3 showed an unusual mode of binding by protruding its heavy chain CDR3 inside the Can f 1 calyx. Epitope mutants generated based on the structural analyses displayed a 64%-89% reduction in IgE antibody binding and failed to induce passive anaphylaxis in a human FcepsilonRIalpha transgenic mouse model. In summary, the structures of Can f 1-hIgE Fab complexes revealed two unique and partially overlapping epitopes on Can f 1. The modification of the identified IgE epitopes provides a pathway for the design of hypoallergens to treat dog allergies. Human IgE monoclonal antibodies define two unusual epitopes trapping dog allergen Can f 1 in different conformations.,Khatri K, Ball A, Glesner J, Linn C, Vailes LD, Wunschmann S, Gabel SA, Zhang J, Peebles RS Jr, Borowski T, Mueller GA, Chapman MD, Smith SA, Pomes A, Chruszcz M Protein Sci. 2025 Sep;34(9):e70269. doi: 10.1002/pro.70269. PMID:40828364 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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