5FK9

Crystal structure of staphylococcal enterotoxin A F47A mutant in complex with a T cell receptor

Summary for 5FK9

• Entry DOI: 10.2210/pdb5fk9/pdb
• Related: 5FKA
• Descriptor: T CELL RECEPTOR ALPHA CHAIN, T CELL RECEPTOR BETA CHAIN, ENTEROTOXIN TYPE A, ... (4 entities in total)
• Functional Keywords: immune system, superantigen, staphylcococcal enterotoxin, t cell receptor, major histocompatibility complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Secreted: 5FK9
• Total number of polymer chains: 3
• Total formula weight: 77632.17

Authors

Rodstrom, K.E.J.,Regenthal, P.,Lindkvist-Petersson, K. (deposition date: 2015-10-15, release date: 2016-05-25, Last modification date: 2024-10-16)

Primary citation

Rodstrom, K.E.J.,Regenthal, P.,Bahl, C.,Ford, A.,Baker, D.,Lindkvist-Petersson, K.
Two Common Structural Motifs for Tcr Recognition by Staphylococcal Enterotoxins
Sci.Rep., 6:25796-, 2016

PubMed Abstract: Superantigens are toxins produced by Staphylococcus aureus, called staphylococcal enterotoxins (abbreviated SEA to SEU). They can cross-link the T cell receptor (TCR) and major histocompatibility complex class II, triggering a massive T cell activation and hence disease. Due to high stability and toxicity, superantigens are potential agents of bioterrorism. Hence, antagonists may not only be useful in the treatment of disease but also serve as countermeasures to biological warfare. Of particular interest are inhibitors against SEA and SEB. SEA is the main cause of food poisoning, while SEB is a common toxin manufactured as a biological weapon. Here, we present the crystal structures of SEA in complex with TCR and SEE in complex with the same TCR, complemented with computational alanine-scanning mutagenesis of SEA, SEB, SEC3, SEE, and SEH. We have identified two common areas that contribute to the general TCR binding for these superantigens. This paves the way for design of single antagonists directed towards multiple toxins.

PubMed: 27180909
DOI: 10.1038/SREP25796

Experimental method

X-RAY DIFFRACTION (3.1 Å)