4UDU

Crystal structure of staphylococcal enterotoxin E in complex with a T cell receptor

Summary for 4UDU

• Entry DOI: 10.2210/pdb4udu/pdb
• Related: 4UDT
• Descriptor: T CELL RECEPTOR ALPHA CHAIN, T-CELL RECEPTOR ALPHA CHAIN C REGION, PROTEIN TRBV7-9, T-CELL RECEPTOR BETA-2 CHAIN C REGION, ENTEROTOXIN TYPE E, ... (6 entities in total)
• Functional Keywords: immune system, superantigen, t cell receptor, major histocompatibility complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane ; Single-pass membrane protein : P01848 A0A5B9; Secreted: P12993
• Total number of polymer chains: 3
• Total formula weight: 77496.29

Authors

Rodstrom, K.E.J.,Regenthal, P.,Lindkvist-Petersson, K. (deposition date: 2014-12-11, release date: 2015-06-24, Last modification date: 2024-10-16)

Primary citation

Rodstrom, K.E.J.,Regenthal, P.,Lindkvist-Petersson, K.
Structure of Staphylococcal Enterotoxin E in Complex with Tcr Defines the Role of Tcr Loop Positioning in Superantigen Recognition.
Plos One, 10:01319-, 2015

PubMed Abstract: T cells are crucial players in cell-mediated immunity. The specificity of their receptor, the T cell receptor (TCR), is central for the immune system to distinguish foreign from host antigens. Superantigens are bacterial toxins capable of inducing a toxic immune response by cross-linking the TCR and the major histocompatibility complex (MHC) class II and circumventing the antigen specificity. Here, we present the structure of staphylococcal enterotoxin E (SEE) in complex with a human T cell receptor, as well as the unligated T cell receptor structure. There are clear structural changes in the TCR loops upon superantigen binding. In particular, the HV4 loop moves to circumvent steric clashes upon complex formation. In addition, a predicted ternary model of SEE in complex with both TCR and MHC class II displays intermolecular contacts between the TCR α-chain and the MHC, suggesting that the TCR α-chain is of importance for complex formation.

PubMed: 26147596
DOI: 10.1371/JOURNAL.PONE.0131988

Experimental method

X-RAY DIFFRACTION (2.5 Å)