Abstract
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.
Original language | English |
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Journal | F E B S Letters |
Volume | 579 |
Issue number | 5 |
Pages (from-to) | 1208-12 |
Number of pages | 5 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 2005 |
Keywords
- 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