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- W2029379074 abstract "Three-dimensional models of the major vicilin allergens from peanut (Ara h 1), lentil (Len c 1) and pea (Pis s 1), were built by homology-based modelling from the X-ray coordinates of the structurally closely related soybean β-conglycinin. All the allergen monomers exhibit the typical cupin motif made of two modules related by a pseudo-dyad axis. Each module consists of a β-barrel core domain associated to a loop domain which mainly contains α-helices. The three cupin motifs are assumed to be arranged in a homotrimeric structure similar to that observed in β-conglycinin, phaseolin or canavalin. Most of the sequential B-cell epitopes characterized on the C-terminus of the Ara h 1 allergen are well conserved in both Len c 1 and Pis s 1 allergens. They occupy very comparable areas on the molecular surface of the allergens and exhibit a similar three-dimensional conformation. This antigenic community readily accounts for the IgE-binding cross-reactivity commonly observed between the vicilin allergens from edible legume seeds. The clinical implication of this cross-reactivity is addressed for a definite diagnosis of legume seed allergy." @default.
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- W2029379074 date "2005-06-01" @default.
- W2029379074 modified "2023-10-18" @default.
- W2029379074 title "Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity" @default.
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- W2029379074 doi "https://doi.org/10.1016/j.biochi.2005.02.011" @default.
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