{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Farquhar R"],"funding":["NIAID NIH HHS","National Health and Medical Research Council","National Institutes of Health","NIAMS NIH HHS","Australian Research Council"],"pagination":["102849"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9900620"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["299(2)"],"pubmed_abstract":["CD1 glycoproteins present lipid-based antigens to T-cell receptors (TCRs). A role for CD1b in T-cell-mediated autoreactivity was proposed when it was established that CD1b can present self-phospholipids with short alkyl chains (∼C34) to T cells; however, the structural characteristics of this presentation and recognition are unclear. Here, we report the 1.9 Å resolution binary crystal structure of CD1b presenting a self-phosphatidylinositol-C34:1 and an endogenous scaffold lipid. Moreover, we also determined the 2.4 Å structure of CD1b-phosphatidylinositol complexed to an autoreactive αβ TCR, BC8B. We show that the TCR docks above CD1b and directly contacts the presented antigen, selecting for both the phosphoinositol headgroup and glycerol neck region via antigen remodeling within CD1b an"],"journal":["The Journal of biological chemistry"],"pubmed_title":["αβ T-cell receptor recognition of self-phosphatidylinositol presented by CD1b."],"pmcid":["PMC9900620"],"funding_grant_id":["2008981","DE210101031","R01 AI049313","R01 AR048632"],"pubmed_authors":["Van Rhijn I","Rossjohn J","Farquhar R","Moody DB","Shahine A"],"additional_accession":[]},"is_claimable":false,"name":"αβ T-cell receptor recognition of self-phosphatidylinositol presented by CD1b.","description":"CD1 glycoproteins present lipid-based antigens to T-cell receptors (TCRs). A role for CD1b in T-cell-mediated autoreactivity was proposed when it was established that CD1b can present self-phospholipids with short alkyl chains (∼C34) to T cells; however, the structural characteristics of this presentation and recognition are unclear. Here, we report the 1.9 Å resolution binary crystal structure of CD1b presenting a self-phosphatidylinositol-C34:1 and an endogenous scaffold lipid. Moreover, we also determined the 2.4 Å structure of CD1b-phosphatidylinositol complexed to an autoreactive αβ TCR, BC8B. We show that the TCR docks above CD1b and directly contacts the presented antigen, selecting for both the phosphoinositol headgroup and glycerol neck region via antigen remodeling within CD1b an","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-04-08T13:16:16.494Z","creation":"2025-04-07T13:01:18.345Z"},"accession":"S-EPMC9900620","cross_references":{"pubmed":["36587766"],"doi":["10.1016/j.jbc.2022.102849"]}}