ArticlePloS one2015
Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Seq2Bind webserver for binding site prediction from sequences using fine-tuned protein language models.NAR genomics and bioinformatics · 2025Article
- Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025Article
- Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells.International journal of molecular sciences · 2022Article
- Computational discovery of binding mode of anti-TRBC1 antibody and predicted key amino acids of TRBC1.Scientific reports · 2022Article
- Structural assessment of HLA-A2-restricted SARS-CoV-2 spike epitopes recognized by public and private T-cell receptors.Nature communications · 2022Article
- IL-15Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Allergy-A New Role for T Cell Superantigens ofToxins · 2020Review
- Antibodies and superantibodies in patients with chronic rhinosinusitis with nasal polyps.The Journal of allergy and clinical immunology · 2017Article
- Thermal stability and structural changes in bacterial toxins responsible for food poisoning.PloS one · 2017Article
- Two common structural motifs for TCR recognition by staphylococcal enterotoxins.Scientific reports · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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