{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ye Y"],"funding":["University of Tennessee","NIAID NIH HHS","National Science Foundation Predoctoral Fellowship","National Cancer Institute","NCI NIH HHS","National Institutes of Health","Novo Nordisk Fonden","National Institute of General Medical Sciences","NIH HHS","NIGMS NIH HHS"],"pagination":["e82861"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10554751"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12"],"pubmed_abstract":["The T cell receptor (TCR) is a complex molecular machine that directs the activation of T cells, allowing the immune system to fight pathogens and cancer cells. Despite decades of investigation, the molecular mechanism of TCR activation is still controversial. One of the leading activation hypotheses is the allosteric model. This model posits that binding of pMHC at the extracellular domain triggers a dynamic change in the transmembrane (TM) domain of the TCR subunits, which leads to signaling at the cytoplasmic side. We sought to test this hypothesis by creating a TM ligand for TCR. Previously we described a method to create a soluble peptide capable of inserting into membranes and binding to the TM domain of the receptor tyrosine kinase EphA2 (Alves et al., eLife, 2018). Here, we show th"],"journal":["eLife"],"pubmed_title":["Allosteric inhibition of the T cell receptor by a designed membrane ligand."],"pmcid":["PMC10554751"],"funding_grant_id":["NNF17OC0028176","R35 GM140846","T32 AI055403","R35GM140846","R35 CA242462","R35CA242462","T32AI055403","DGE- 2139841"],"pubmed_authors":["Chang JJ","Wilhelm KB","Barrera FN","DiMaio D","Ye Y","Morita S","Groves JT","Buckley PM"],"additional_accession":[]},"is_claimable":false,"name":"Allosteric inhibition of the T cell receptor by a designed membrane ligand.","description":"The T cell receptor (TCR) is a complex molecular machine that directs the activation of T cells, allowing the immune system to fight pathogens and cancer cells. Despite decades of investigation, the molecular mechanism of TCR activation is still controversial. One of the leading activation hypotheses is the allosteric model. This model posits that binding of pMHC at the extracellular domain triggers a dynamic change in the transmembrane (TM) domain of the TCR subunits, which leads to signaling at the cytoplasmic side. We sought to test this hypothesis by creating a TM ligand for TCR. Previously we described a method to create a soluble peptide capable of inserting into membranes and binding to the TM domain of the receptor tyrosine kinase EphA2 (Alves et al., eLife, 2018). Here, we show th","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Oct","modification":"2026-05-29T03:59:41.454Z","creation":"2024-12-04T13:15:32.09Z"},"accession":"S-EPMC10554751","cross_references":{"pubmed":["37796108"],"doi":["10.7554/eLife.82861"]}}