scholarly journals Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

10.3791/54991 ◽  
2017 ◽  
Author(s):  
Bruce J. MacLachlan ◽  
Alexander Greenshields-Watson ◽  
Georgina H Mason ◽  
Andrea J Schauenburg ◽  
Valentina Bianchi ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
X Ray ◽  
X Ray Crystallography ◽  
Functional Assays ◽  
Cancer Antigens ◽  
Receptor Recognition

scholarly journals Selective Inhibitors of T Cell Receptor Recognition of Antigen–MHC Complexes for Rheumatoid Arthritis

2019 ◽  
Vol 10 (4) ◽  
pp. 644-649
Author(s):  
Francesco Ria ◽  
Davide Pirolli ◽  
Gabriele Di Sante ◽  
Benedetta Righino ◽  
Elisa Gremese ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Selective Inhibitors ◽  
Receptor Recognition

scholarly journals Atypical TRAV1-2− T cell receptor recognition of the antigen-presenting molecule MR1

2020 ◽  
Vol 295 (42) ◽  
pp. 14445-14457 ◽  
Author(s):  
Wael Awad ◽  
Erin W. Meermeier ◽  
Maria L. Sandoval-Romero ◽  
Jérôme Le Nours ◽  
Aneta H. Worley ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
T Cell Repertoire ◽  
Cell Repertoire ◽  
Mait Cells ◽  
Receptor Recognition ◽  
Antigen Presenting ◽  
Β Chain ◽  
Complementarity Determining Region

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.

scholarly journals Divergent T-cell receptor recognition modes of a HLA-I restricted extended tumour-associated peptide

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Kok Fei Chan ◽  
Benjamin S. Gully ◽  
Stephanie Gras ◽  
Dennis X. Beringer ◽  
Lars Kjer-Nielsen ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Receptor Recognition
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