Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity
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The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.
|Journal||F E B S Letters|
|Number of pages||5|
|Publication status||Published - 2005|
- Allergens, Animals, Antigens, Dermatophagoides, Arthropod Proteins, Cross Reactions, Crystallography, X-Ray, Epitopes, Hydrophobic and Hydrophilic Interactions, Immunoglobulin E, Lipid Metabolism, Models, Molecular, Protein Structure, Tertiary, Pyroglyphidae