1LO5

Crystal structure of the D227A variant of Staphylococcal enterotoxin A in complex with human MHC class II

Summary for 1LO5

• Entry DOI: 10.2210/pdb1lo5/pdb
• Related: 1dlh 1esf
• Descriptor: HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DR-1 beta chain, Hemagglutinin peptide, ... (5 entities in total)
• Functional Keywords: protein-protein 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: P0A0L2
• Total number of polymer chains: 4
• Total formula weight: 71829.67

Authors

Petersson, K.,Thunnissen, M.,Forsberg, G.,Walse, B. (deposition date: 2002-05-06, release date: 2002-12-18, Last modification date: 2024-10-09)

Primary citation

Petersson, K.,Thunnissen, M.,Forsberg, G.,Walse, B.
Crystal Structure of a SEA Variant in Complex with MHC Class II Reveals the Ability of SEA to Crosslink MHC Molecules
Structure, 10:1619-1626, 2002

PubMed Abstract: 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.

PubMed: 12467569
DOI: 10.1016/S0969-2126(02)00895-X

Experimental method

X-RAY DIFFRACTION (3.2 Å)