5jt8

Structural basis for the limited antibody cross reactivity between the mite allergens Blo t 1 and Der p 1

spinqualitylabelsall models 5jt8, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jt8 is a 2 chain structure with sequence from Blomia tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CL, CSO, NAG, NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CYSP_BLOTA Cysteine protease.[UniProtKB:A5HII1] Publication Abstract from PubMed The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic asthma and rhinitis in tropical and subtropical regions. Here, we report the crystal structure of one of the allergens from Blo t, recombinant proBlo t 1 (rproBlo t 1), determined at 2.1 A resolution. Overall, the fold of rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG epitopes to the same surface patch on Blo t 1, as well as of sequence identity of surface-exposed residues, suggests limited cross-reactivity between these allergens and Blo t 1. This is in agreement with ELISA inhibition results showing that, although cross-reactive human IgE epitopes exist, there are unique IgE epitopes for both Blo t 1 and Der p 1. The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1.,Meno KH, Kastrup JS, Kuo IC, Chua KY, Gajhede M Allergy. 2017 Apr;72(4):665-670. doi: 10.1111/all.13111. Epub 2017 Jan 19. PMID:27997997 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA