Journal
IMMUNITY
Volume 14, Issue 1, Pages 93-103Publisher
CELL PRESS
DOI: 10.1016/S1074-7613(01)00092-9
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Funding
- NIAID NIH HHS [AI42937, AI36900] Funding Source: Medline
- PHS HHS [36611] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R37AI036900, R01AI036900] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [Z01OD010485] Funding Source: NIH RePORTER
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MHC class II molecules possess two binding sites for bacterial superantigens (SAGs): a low-affinity site on the cu chain and a high-affinity, zinc-dependent site on the beta chain. only the former has been defined crystallographically. We report the structure of streptococcal pyrogenic exotoxin C (SPE-C) complexed with HLA-DR2a (DRA*010l, DRB5*0101) bearing a self-peptide from myelin basic protein (MBP). SPE-C binds the beta chain through a zinc bridge that links the SAG and class II molecules. Surprisingly, SPE-C also makes extensive contacts with the MBP peptide, such that peptide accounts for one third of the surface area of the MHC molecule buried in the complex, similar to TCR-peptide/MHC complexes. Thus, SPE-C may optimize T cell responses by mimicking the peptide dependence of conventional antigen presentation and recognition.
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