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Atypical TRAV1-2
- Source :
- J Biol Chem
- Publication Year :
- 2020
-
Abstract
- MR1 presents vitamin B–related metabolites to mucosal associated invariant T (MAIT) cells, which are characterized, in part, by the TRAV1-2(+) αβ T cell receptor (TCR). In addition, a more diverse TRAV1-2(−) MR1-restricted T cell repertoire exists that can possess altered specificity for MR1 antigens. However, the molecular basis of how such TRAV1-2(−) TCRs interact with MR1–antigen complexes remains unclear. Here, we describe how a TRAV12-2(+) TCR (termed D462-E4) recognizes an MR1–antigen complex. We report the crystal structures of the unliganded D462-E4 TCR and its complex with MR1 presenting the riboflavin-based antigen 5-OP-RU. Here, the TRBV29-1 β-chain of the D462-E4 TCR binds over the F′-pocket of MR1, whereby the complementarity-determining region (CDR) 3β loop surrounded and projected into the F′-pocket. Nevertheless, the CDR3β loop anchored proximal to the MR1 A′-pocket and mediated direct contact with the 5-OP-RU antigen. The D462-E4 TCR footprint on MR1 contrasted that of the TRAV1-2(+) and TRAV36(+) TCRs' docking topologies on MR1. Accordingly, diverse MR1-restricted T cell repertoire reveals differential docking modalities on MR1, thus providing greater scope for differing antigen specificities.
- Subjects :
- Antigen Presentation
Binding Sites
Receptors, Antigen, T-Cell, alpha-beta
T-Lymphocytes
Histocompatibility Antigens Class I
Immunology
Surface Plasmon Resonance
Crystallography, X-Ray
Protein Refolding
Protein Structure, Tertiary
Minor Histocompatibility Antigens
Molecular Docking Simulation
Humans
Amino Acid Sequence
Uracil
Ribitol
Subjects
Details
- ISSN :
- 1083351X
- Volume :
- 295
- Issue :
- 42
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.pmid..........4196e762136d6d24db60753e3e72c8b6