1L0X

TCR beta chain complexed with streptococcal superantigen SpeA

Summary for 1L0X

• Entry DOI: 10.2210/pdb1l0x/pdb
• Related: 1JCK 1L0Y 1SBB
• Descriptor: 14.3.d T cell receptor beta chain, Exotoxin type A, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tcr, superantigen, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass membrane protein (Potential): P01851
• Total number of polymer chains: 4
• Total formula weight: 105021.13

Authors

Li, H.,Sundberg, E.J.,Mariuzza, R.A. (deposition date: 2002-02-14, release date: 2002-04-03, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)