1HXY

CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II

Summary for 1HXY

• Entry DOI: 10.2210/pdb1hxy/pdb
• Related: 1DLH 1ENF 1EWZ
• Descriptor: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN, HEMAGGLUTININ, ... (6 entities in total)
• Functional Keywords: complex, immune system-toxin complex, immune system/toxin
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01903 P04229; Secreted: P0A0M0
• Total number of polymer chains: 4
• Total formula weight: 69502.35

Authors

Petersson, K.,Hakansson, M.,Nilsson, H.,Forsberg, G.,Svensson, L.A.,Liljas, A.,Walse, B. (deposition date: 2001-01-17, release date: 2001-06-27, Last modification date: 2024-10-16)

Primary citation

Petersson, K.,Hakansson, M.,Nilsson, H.,Forsberg, G.,Svensson, L.A.,Liljas, A.,Walse, B.
Crystal Structure of a Superantigen Bound to MHC Class II Displays Zinc and Peptide Dependence
Embo J., 20:3306-3312, 2001

PubMed Abstract: 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.

PubMed: 11432818
DOI: 10.1093/emboj/20.13.3306

Experimental method

X-RAY DIFFRACTION (2.6 Å)