Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules
Författare
Summary, in English
Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy.
Publiceringsår
2002
Språk
Engelska
Sidor
1619-1626
Publikation/Tidskrift/Serie
Structure
Volym
10
Issue
12
Dokumenttyp
Artikel i tidskrift
Förlag
Cell Press
Ämne
- Biological Sciences
Nyckelord
- enterotoxin
- staphylococcal
- SEA
- MHC class II
- protein-protein interaction
- superantigen
- X-ray crystallography
Status
Published
Forskningsgrupp
- Medical Structural Biology
ISBN/ISSN/Övrigt
- ISSN: 0969-2126