TCRs bind to CD1b-PG complexes formed in cells.

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Comparison of ternary TCR-lipid-CD1 complex structures.
The functional and structural basis of phospholipid recognition by the PG90 TCR. The functional and structural basis of phospholipid recognition by the.
Docking footprint of PG90 TCR on CD1b-PG.
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Comparison of ternary TCR-lipid-CD1 complex structures.
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Ligands eluted from hpMR1+EC and hpMR1+MS contain both shared and unique ions. Ligands eluted from hpMR1+EC and hpMR1+MS contain both shared and unique.
GNPS assists in the identification of novel hpMR1 eluted ions.
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MR1T clones with distinct TCR usage display differential recognition of discrete activating ligands. MR1T clones with distinct TCR usage display differential.
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TCRs bind to CD1b-PG complexes formed in cells. TCRs bind to CD1b-PG complexes formed in cells. (A) Cellular phospholipids share a PA core structure. PG, PC, PE, PS, and PI are distinguished by head groups above the dotted line. (B) C1R cells transfected with CD1a or CD1b were pulsed with the indicated lipid and stained with PG90 or GEM42 TCR tetramers. Gating strategy is shown in fig. S2. (C) Total cellular lipids were extracted from human monocyte-derived DCs, C1R cells, and K562 cells, separated using normal-phase HPLC, and detected as ion chromatograms that match the mass values for PG (m/z 775.5 and 747.5), which were previously established from TLC-MS. (D) MS signals for the abundant species of PG, PE, and PC. Experiments in (B) and (C) were performed at least twice, with similar results. Measurements in (D) were performed once in each of the three cell types. Adam Shahine et al. Sci. Immunol. 2017;2:eaao1384 Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).