Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity

Research output: Contribution to journalJournal articleResearchpeer-review

Birthe R Johannessen, Lars Skov, Jette S Kastrup, Ole Kristensen, Caroline Bolwig, Jørgen Larsen, Michael Spangfort, Kaare Lund, Michael Gajhede

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 languageEnglish
JournalF E B S Letters
Volume579
Issue number5
Pages (from-to)1208-12
Number of pages5
ISSN0014-5793
DOIs
Publication statusPublished - 2005

    Research areas

  • 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

ID: 40318547