Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity |
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| Authors: | Johannessen Birthe R Skov Lars K Kastrup Jette S Kristensen Ole Bolwig Caroline Larsen Jørgen N Spangfort Michael Lund Kaare Gajhede Michael |
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| Affiliation: | Biostructural Research, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark. |
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| 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. |
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| Keywords: | Eur m 2, Euroglyphus maynei major allergen 2 GM2-AP, GM2-activator protein HE1, human epidymal secretory protein IgE, immunoglobulin E Lep d 2, major type 2 allergen Lepidoglyphus destructor Der f 2, major type 2 allergen from Dermatophagoides farinae Der p 2, major type 2 allergen from Dermatophagoides pteronyssinus ML, MD-2-related lipid-recognition MR, molecular replacement PEG, Polyethylene glycol RhoGDI, Rho-specific guanine dissociation inhibitor RMSD, root mean square deviation |
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