
The structure determination of major allergens is a prerequisite for analyzing surface exposed areas of the allergen and for mapping conformational epitopes. These may be determined by experimental methods including crystallographic and NMR-based approaches or predicted by computational methods. In this review we summarize the existing structural information on allergens and their classification in protein fold families. The currently available allergen-antibody complexes are described and the experimentally obtained epitopes compared. Furthermore we discuss established methods for linear and conformational epitope mapping, putting special emphasis on a recently developed approach, which uses the structural similarity of proteins in combination with the experimental cross-reactivity data for epitope prediction.
Models, Molecular, info:eu-repo/classification/ddc/540, Biochemistry, Genetics and Molecular Biology(all), Recombinant Fusion Proteins, Allergens, Crystallography, X-Ray, Article, Protein Structure, Secondary, Protein Structure, Tertiary, Epitopes, Hypersensitivity, Animals, Humans, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Epitope Mapping, Software
Models, Molecular, info:eu-repo/classification/ddc/540, Biochemistry, Genetics and Molecular Biology(all), Recombinant Fusion Proteins, Allergens, Crystallography, X-Ray, Article, Protein Structure, Secondary, Protein Structure, Tertiary, Epitopes, Hypersensitivity, Animals, Humans, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Epitope Mapping, Software
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