1JCK

T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SEC3 SUPERANTIGEN

1JCK の概要

• エントリーDOI: 10.2210/pdb1jck/pdb
• 分子名称: 14.3.D T CELL ANTIGEN RECEPTOR, STAPHYLOCOCCAL ENTEROTOXIN C3 (2 entities in total)
• 機能のキーワード: t-cell, receptor, transmembrane, glycoprotein, enterotoxin, toxin, superantigen, complex (toxin-receptor), complex (toxin-receptor) complex, complex (toxin/receptor)
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Secreted: P0A0L5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108465.02

構造登録者

Fields, B.A.,Mariuzza, R.A. (登録日: 1996-10-22, 公開日: 1997-11-12, 最終更新日: 2024-10-23)

主引用文献

Fields, B.A.,Malchiodi, E.L.,Li, H.,Ysern, X.,Stauffacher, C.V.,Schlievert, P.M.,Karjalainen, K.,Mariuzza, R.A.
Crystal structure of a T-cell receptor beta-chain complexed with a superantigen.
Nature, 384:188-192, 1996

PubMed Abstract: Superantigens (SAgs) are viral or bacterial proteins that act as potent T-cell stimulants and have been implicated in a number of human diseases, including toxic shock syndrome, diabetes mellitus and multiple sclerosis. The interaction of SAgs with the T-cell receptor (TCR) and major histocompatibility complex (MHC) proteins results in the stimulation of a disproportionately large fraction of the T-cell population. We report here the crystal structures of the beta-chain of a TCR complexed with the Staphylococcus aureus enterotoxins C2 and C3 (SEC2, SEC3). These enterotoxins, which cause both toxic shock and food poisoning, bind in an identical way to the TCR beta-chain. The complementarity-determining region 2 (CDR2) of the beta-chain and, to lesser extents, CDR1 and hypervariable region 4 (HV4), bind in a cleft between the two domains of the SAgs. Thus, there is considerable overlap between the SAg-binding site and the peptide/MHC-binding sites of the TCR. A model of a TCR-SAg-MHC complex constructed from the crystal structures of (1) the beta-chain-SEC3 complex, (2) a complex between staphylococcal enterotoxin B (SEB) and an MHC molecule, and (3) a TCR V(alpha) domain, reveals that the SAg acts as a wedge between the TCR and MHC to displace the antigenic peptide away from the TCR combining site. In this way, the SAg is able to circumvent the normal mechanism for T-cell activation by specific peptide/MHC complexes.

PubMed: 8906797
DOI: 10.1038/384188a0

実験手法

X-RAY DIFFRACTION (3.5 Å)