4AKA
IPSE alpha-1, an IgE-binding crystallin
4AKA の概要
| エントリーDOI | 10.2210/pdb4aka/pdb |
| NMR情報 | BMRB: 17405 |
| 分子名称 | IL-4-INDUCING PROTEIN (1 entity in total) |
| 機能のキーワード | immune system, schistosoma mansoni, immunoglobulin binding |
| 由来する生物種 | SCHISTOSOMA MANSONI (BLOOD FLUKE) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11981.48 |
| 構造登録者 | Meyer, N.H.,Mayerhofer, H.,Tripsianes, K.,Barths, D.,Blindow, S.,Bade, S.,Madl, T.,Frey, A.,Haas, H.,Mueller-Dieckmann, J.,Sattler, M.,Scharmm, G. (登録日: 2012-02-22, 公開日: 2013-03-13, 最終更新日: 2024-11-13) |
| 主引用文献 | Meyer, N.H.,Mayerhofer, H.,Tripsianes, K.,Barths, D.,Blindow, S.,Bade, S.,Madl, T.,Frey, A.,Haas, H.,Mueller-Dieckmann, J.,Sattler, M.,Scharmm, G. A Crystallin Fold in the Interleukin-4-Inducing Principle of Schistosoma Mansoni Eggs (Ipse/Alpha-1) Mediates Ige Binding for Antigen-Independent Basophil Activation J.Biol.Chem., 290:22111-, 2015 Cited by PubMed Abstract: The IL-4-inducing principle from Schistosoma mansoni eggs (IPSE/α-1), the major secretory product of eggs from the parasitic worm S. mansoni, efficiently triggers basophils to release the immunomodulatory key cytokine interleukin-4. Activation by IPSE/α-1 requires the presence of IgE on the basophils, but the detailed molecular mechanism underlying activation is unknown. NMR and crystallographic analysis of IPSEΔNLS, a monomeric IPSE/α-1 mutant, revealed that IPSE/α-1 is a new member of the βγ-crystallin superfamily. We demonstrate that this molecule is a general immunoglobulin-binding factor with highest affinity for IgE. NMR binding studies of IPSEΔNLS with the 180-kDa molecule IgE identified a large positively charged binding surface that includes a flexible loop, which is unique to the IPSE/α-1 crystallin fold. Mutational analysis of amino acids in the binding interface showed that residues contributing to IgE binding are important for IgE-dependent activation of basophils. As IPSE/α-1 is unable to cross-link IgE, we propose that this molecule, by taking advantage of its unique IgE-binding crystallin fold, activates basophils by a novel, cross-linking-independent mechanism. PubMed: 26163514DOI: 10.1074/JBC.M115.675066 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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