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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Allergens / chemistry*
-
Allergens / immunology*
-
Animals
-
Antigens, Dermatophagoides / chemistry*
-
Antigens, Dermatophagoides / immunology*
-
Arthropod Proteins
-
Cross Reactions / immunology*
-
Crystallography, X-Ray
-
Epitopes / immunology
-
Hydrophobic and Hydrophilic Interactions
-
Immunoglobulin E / immunology*
-
Lipid Metabolism
-
Models, Molecular
-
Protein Structure, Tertiary
-
Pyroglyphidae / chemistry*
-
Pyroglyphidae / immunology
Substances
-
Allergens
-
Antigens, Dermatophagoides
-
Arthropod Proteins
-
Dermatophagoides farinae antigen f 2
-
Epitopes
-
Immunoglobulin E