4udu | pdb_00004udu
From Proteopedia
Crystal structure of staphylococcal enterotoxin E in complex with a T cell receptor
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Structural highlights
Function[ETXE_STAAU] Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death. Publication Abstract from PubMedT 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 alpha-chain and the MHC, suggesting that the TCR alpha-chain is of importance for complex formation. Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.,Rodstrom KE, Regenthal P, Lindkvist-Petersson K PLoS One. 2015 Jul 6;10(7):e0131988. doi: 10.1371/journal.pone.0131988., eCollection 2015. PMID:26147596[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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