1L0X

TCR beta chain complexed with streptococcal superantigen SpeA

1L0X の概要

• エントリーDOI: 10.2210/pdb1l0x/pdb
• 関連するPDBエントリー: 1JCK 1L0Y 1SBB
• 分子名称: 14.3.d T cell receptor beta chain, Exotoxin type A, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: tcr, superantigen, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass membrane protein (Potential): P01851
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105021.13

構造登録者

Li, H.,Sundberg, E.J.,Mariuzza, R.A. (登録日: 2002-02-14, 公開日: 2002-04-03, 最終更新日: 2024-11-20)

主引用文献

Sundberg, E.J.,Li, H.,Llera, A.S.,McCormick, J.K.,Tormo, J.,Schlievert, P.M.,Karjalainen, K.,Mariuzza, R.A.
Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes.
Structure, 10:687-699, 2002

PubMed Abstract: Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.

PubMed: 12015151
DOI: 10.1016/S0969-2126(02)00759-1

実験手法

X-RAY DIFFRACTION (2.8 Å)