Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873686 | FEBS Letters | 2005 | 5 Pages |
Abstract
The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83Â Ã
resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel β-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.
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Authors
Birthe R. Johannessen, Lars K. Skov, Jette S. Kastrup, Ole Kristensen, Caroline Bolwig, Jørgen N. Larsen, Michael Spangfort, Kaare Lund, Michael Gajhede,