3OWE
Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a High Affinity Mutant Mouse T-cell Receptor Chain
3OWE の概要
| エントリーDOI | 10.2210/pdb3owe/pdb |
| 関連するPDBエントリー | 1XXG 3MC0 |
| 分子名称 | Beta-chain, Enterotoxin SEG (3 entities in total) |
| 機能のキーワード | t-cell receptor v beta domain, complex structure, igg domains, b grasp, virulence factors, immune system |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| タンパク質・核酸の鎖数 | 16 |
| 化学式量合計 | 313512.39 |
| 構造登録者 | Fernandez, M.M.,Cho, S.,Robinson, H.,Mariuzza, R.A.,Malchiodi, M.L. (登録日: 2010-09-17, 公開日: 2010-11-03, 最終更新日: 2024-10-16) |
| 主引用文献 | Fernandez, M.M.,Cho, S.,De Marzi, M.C.,Kerzic, M.C.,Robinson, H.,Mariuzza, R.A.,Malchiodi, E.L. Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain. J.Biol.Chem., 286:1189-1195, 2011 Cited by PubMed Abstract: Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host. PubMed: 21059660DOI: 10.1074/jbc.M110.142471 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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