期刊
FEBS LETTERS
卷 579, 期 5, 页码 1208-1212出版社
WILEY
DOI: 10.1016/j.febslet.2004.11.115
关键词
Dermatophagoides farinae group 2 major allergen; cross-reacting epitope; hydrophobic cavity; lipid binding
The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 Angstrom 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. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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