2B90
Crystal structure of the interleukin-4 variant T13DR85A
2B90 の概要
エントリーDOI | 10.2210/pdb2b90/pdb |
関連するPDBエントリー | 2B8U 2B8X 2B8Y 2B8Z 2B91 2D48 |
分子名称 | Interleukin-4, SULFATE ION (3 entities in total) |
機能のキーワード | four helix bundle, cytokine |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Secreted: P05112 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 15205.30 |
構造登録者 | Kraich, M.,Klein, M.,Patino, E.,Harrer, H.,Sebald, W.,Mueller, T.D. (登録日: 2005-10-10, 公開日: 2006-05-30, 最終更新日: 2024-10-23) |
主引用文献 | Kraich, M.,Klein, M.,Patino, E.,Harrer, H.,Nickel, J.,Sebald, W.,Mueller, T.D. A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor Bmc Biol., 4:13-13, 2006 Cited by PubMed Abstract: Interleukin 4 (IL-4) is a key regulator of the immune system and an important factor in the development of allergic hypersensitivity. Together with interleukin 13 (IL-13), IL-4 plays an important role in exacerbating allergic and asthmatic symptoms. For signal transduction, both cytokines can utilise the same receptor, consisting of the IL-4Ralpha and the IL-13Ralpha1 chain, offering an explanation for their overlapping biological functions. Since both cytokine ligands share only moderate similarity on the amino acid sequence level, molecular recognition of the ligands by both receptor subunits is of great interest. IL-4 and IL-13 are interesting targets for allergy and asthma therapies. Knowledge of the binding mechanism will be important for the generation of either IL-4 or IL-13 specific drugs. PubMed: 16640778DOI: 10.1186/1741-7007-4-13 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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