1ktk
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(New page: 200px<br /> <applet load="1ktk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktk, resolution 3.00Å" /> '''Complex of Streptoc...)
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Revision as of 15:48, 12 November 2007
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Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)
Overview
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 Structure
1KTK is a Protein complex structure of sequences from Homo sapiens and Streptococcus pyogenes. Full crystallographic information is available from OCA.
Reference
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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