2NTS

Crystal Structure of SEK-hVb5.1

2NTS の概要

• エントリーDOI: 10.2210/pdb2nts/pdb
• 関連するPDBエントリー: 2NTT
• 分子名称: TRBC1 protein, Staphylococcal enterotoxin K (3 entities in total)
• 機能のキーワード: superantigen; t cell receptor, toxin-immune system complex, toxin/immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52214.82

構造登録者

Gunther, S.,Varma, A.K.,Moza, B.,Sundberg, E.J. (登録日: 2006-11-08, 公開日: 2007-06-26, 最終更新日: 2024-11-20)

主引用文献

Gunther, S.,Varma, A.K.,Moza, B.,Kasper, K.J.,Wyatt, A.W.,Zhu, P.,Rahman, A.K.,Li, Y.,Mariuzza, R.A.,McCormick, J.K.,Sundberg, E.J.
A novel loop domain in superantigens extends their T cell receptor recognition site
J.Mol.Biol., 371:210-221, 2007

PubMed Abstract: Superantigens (SAGs) interact with host immune receptors to induce a massive release of inflammatory cytokines that can lead to toxic shock syndrome and death. Bacterial SAGs can be classified into five distinct evolutionary groups. Group V SAGs are characterized by the alpha3-beta8 loop, a unique approximately 15 amino acid residue extension that is required for optimal T cell activation. Here, we report the X-ray crystal structures of the group V SAG staphylococcal enterotoxin K (SEK) alone and in complex with the TCR hVbeta5.1 domain. SEK adopts a unique TCR binding orientation relative to other SAG-TCR complexes, which results in the alpha3-beta8 loop contacting the apical loop of framework region 4, thereby extending the known TCR recognition site of SAGs. These interactions are absolutely required for TCR binding and T cell activation by SEK, and dictate the TCR Vbeta domain specificity of SEK and other group V SAGs.

PubMed: 17560605
DOI: 10.1016/j.jmb.2007.05.038

実験手法

X-RAY DIFFRACTION (2.4 Å)