1l0x
TCR beta chain complexed with streptococcal superantigen SpeA
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OverviewOverview
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.
About this StructureAbout this Structure
1L0X is a Protein complex structure of sequences from Mus musculus and Streptococcus pyogenes with GOL as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes., Sundberg EJ, Li H, Llera AS, McCormick JK, Tormo J, Schlievert PM, Karjalainen K, Mariuzza RA, Structure. 2002 May;10(5):687-99. PMID:12015151
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