Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity.
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.
Johannessen
Birthe R
BR
Biostructural Research, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
Skov
Lars K
LK
Kastrup
Jette S
JS
Kristensen
Ole
O
Bolwig
Caroline
C
Larsen
Jørgen N
JN
Spangfort
Michael
M
Lund
Kaare
K
Gajhede
Michael
M
D000485:Allergens / Q000737:chemistry* / Q000276:immunology*; D000818:Animals; D039741:Antigens, Dermatophagoides / Q000737:chemistry* / Q000276:immunology*; D060829:Arthropod Proteins; D003429:Cross Reactions / Q000276:immunology*; D018360:Crystallography, X-Ray; D000939:Epitopes / Q000276:immunology; D057927:Hydrophobic and Hydrophilic Interactions; D007073:Immunoglobulin E / Q000276:immunology*; D050356:Lipid Metabolism; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D039981:Pyroglyphidae / Q000737:chemistry* / Q000276:immunology
D000485:Allergens; D039741:Antigens, Dermatophagoides; D060829:Arthropod Proteins; C451160:Dermatophagoides farinae antigen f 2; D000939:Epitopes; D007073:Immunoglobulin E