2F08
Crystal structure of a major house dust mite allergen, Derf 2
2F08 の概要
| エントリーDOI | 10.2210/pdb2f08/pdb |
| 分子名称 | mite allergen Der f II, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL (3 entities in total) |
| 機能のキーワード | immunoglobulin fold, immune system |
| 由来する生物種 | Dermatophagoides farinae (American house dust mite) |
| 細胞内の位置 | Secreted: Q00855 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 56581.14 |
| 構造登録者 | Mikami, B.,Tanaka, Y.,Minato, N.,Suzuki, M.,Korematsu, S. (登録日: 2005-11-12, 公開日: 2005-11-29, 最終更新日: 2024-11-13) |
| 主引用文献 | Suzuki, M.,Tanaka, Y.,Korematsu, S.,Mikami, B.,Minato, N. Crystal structure and some properties of a major house dust mite allergen, Derf 2 Biochem.Biophys.Res.Commun., 339:679-686, 2006 Cited by PubMed Abstract: Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1A resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens. PubMed: 16313885DOI: 10.1016/j.bbrc.2005.11.065 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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