Summary
PDB 1HXY deposited: 2001-01-17 modified: 2009-02-24
Title CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II
Authors Forsberg, G., Hakansson, M., Liljas, A., Nilsson, H., Petersson, K., Svensson, L.A., Walse, B.
Method X-RAY DIFFRACTION
Structure factors resolution 2.6 rfactor 0.202 rfree 0.258
DPI 0.89 theoretical min: 0.40
Citations

The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.

EMBO J. 2001 Jul 2;20(13):3306-12.

Cross References
Database source Identifier Description
PubMed 11432818 EMJODG
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1HXY/1 1HXY 1 tetramer 0 4 1 4521