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Title: Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity. Author: Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M. Journal: FEBS Lett; 2005 Feb 14; 579(5):1208-12. PubMed ID: 15710415. 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.[Abstract] [Full Text] [Related] [New Search]