4C56

X-ray structure of the complex between staphylococcal enterotoxin B, T cell receptor and major histocompatibility complex class II

Summary for 4C56

• Entry DOI: 10.2210/pdb4c56/pdb
• Descriptor: T CELL RECEPTOR ALPHA CHAIN, T CELL RECEPTOR BETA CHAIN, ENTEROTOXIN B, ... (8 entities in total)
• Functional Keywords: immune system-toxin complex, immune system/toxin
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: Q5MAA8; Virion membrane; Single-pass type I membrane protein (Potential): A9JJF6
• Total number of polymer chains: 12
• Total formula weight: 247308.55

Authors

Rodstrom, K.E.J.,Elbing, K.,Lindkvist-Petersson, K. (deposition date: 2013-09-10, release date: 2014-07-23, Last modification date: 2023-12-20)

Primary citation

Rodstrom, K.E.J.,Elbing, K.,Lindkvist-Petersson, K.
Structure of the Superantigen Staphylococcal Enterotoxin B in Complex with Tcr and Peptide-Mhc Demonstrates Absence of Tcr-Peptide Contacts.
J.Immunol., 193:1998-, 2014

PubMed Abstract: Superantigens are immune-stimulatory toxins produced by Staphylococcus aureus, which are able to interact with host immune receptors to induce a massive release of cytokines, causing toxic shock syndrome and possibly death. In this article, we present the x-ray structure of staphylococcal enterotoxin B (SEB) in complex with its receptors, the TCR and MHC class II, forming a ternary complex. The structure, in combination with functional analyses, clearly shows how SEB adopts a wedge-like position when binding to the β-chain of TCR, allowing for an interaction between the α-chain of TCR and MHC. Furthermore, the binding mode also circumvents contact between TCR and the peptide presented by MHC, which enables SEB to initiate a peptide-independent activation of T cells.

PubMed: 25015819
DOI: 10.4049/JIMMUNOL.1401268

Experimental method

X-RAY DIFFRACTION (2.9 Å)