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PDBsum entry 4udt

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Immune system PDB id
4udt
Contents
Protein chains
202 a.a.
241 a.a.
Ligands
GOL
Waters ×309

References listed in PDB file
Key reference
Title Structure of staphylococcal enterotoxin e in complex with tcr defines the role of tcr loop positioning in superantigen recognition.
Authors K.E.Rödström, P.Regenthal, K.Lindkvist-Petersson.
Ref. Plos One, 2015, 10, e0131988. [DOI no: 10.1371/journal.pone.0131988]
PubMed id 26147596
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.
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