1. The functional and structural basis of phospholipid recognition by the PG90 TCR.
The functional and structural basis of phospholipid recognition by the PG90 TCR. (A) Staining of the PG90 cell line by CD1b tetramers with a single alanine mutant at the indicated site with or without bound PG. Residues interacting with the PG90 TCR are highlighted in blue. MFI, mean fluorescence intensity. (B) Color coding summary: white, not tested; dark gray, no effect (<25% reduction); orange, moderate effect (25 to 75% reduction); red, markedly reduced binding (>75% reduction). (C) Electrostatic potential of the cationic cup. The potential contours are shown on a scale from (positive charge, blue) to −10.0 kBT e−1 (negative charge, red); white indicates a value close to 0 kBT e−1 (neutral charge). (D) Side view of hydrogen bond network between PG (green) and PG90 TCR, with CDR1α, CDR3α, and CDR3β loops represented in teal, purple, and yellow, respectively. Contacts with the head group of PG (E) and GMM (F). The interactions are represented as red dashes, whereas the cyan dash represents the hydrogen bond (E), and salt bridge (F), that forms the arginine capstone.
Adam Shahine et al. Sci. Immunol. 2017;2:eaao1384
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