1XWV
Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity
Summary for 1XWV
Entry DOI | 10.2210/pdb1xwv/pdb |
Descriptor | Der f II, 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL, 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL, ... (4 entities in total) |
Functional Keywords | beta sheets, allergen |
Biological source | Dermatophagoides farinae (American house dust mite) |
Cellular location | Secreted: Q00855 |
Total number of polymer chains | 2 |
Total formula weight | 29201.65 |
Authors | Johannessen, B.R.,Skov, L.K.,Kastrup, J.S.,Kristensen, O.,Bolwig, C.,Larsen, J.N.,Spangfort, M.,Lund, K.,Gajhede, M. (deposition date: 2004-11-02, release date: 2004-12-14, Last modification date: 2024-11-06) |
Primary citation | Johannessen, B.R.,Skov, L.K.,Kastrup, J.S.,Kristensen, O.,Bolwig, C.,Larsen, J.N.,Spangfort, M.,Lund, K.,Gajhede, M. Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity. Febs Lett., 579:1208-1212, 2005 Cited by PubMed 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. PubMed: 15710415DOI: 10.1016/j.febslet.2004.11.115 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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