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. Author manuscript; available in PMC: 2021 Feb 23.
Published in final edited form as: Nat Struct Mol Biol. 2017 Feb 20;24(4):387–394. doi: 10.1038/nsmb.3381

Figure 6.

Figure 6

HLA-B*57:01 TW10 and T3N binding to KIR3DL1. (a) (i) Representative surface plasmon resonance (SPR) injection series from two independent experiments for KIR3DL1 binding to the TW10 (top) and T3N (bottom) HLA-B*57:01 complexes. (ii,iii) SPR-based affinity measurements of the interaction between KIR3DL1*001 and B57:01 T3N (ii) and B*57:01 TW10 (iii) complexes; results represent two independent experiments. Data are shown as mean ± range of two values. Concentration values represent the equilibrium binding constants of KIR3DL1 for the HLA-peptide complexes. RU, response units. (b) Staining of KIR3DL1 allotypes with HLA-B*57:01 TW10 (orange) and T3N (blue) tetramers (0.2 μg each), normalized to TW10 binding. Results represent two (015), three (005) and four (001) independent replicates. Data are shown as mean ± range. (c,d) HLA-B*57:01 TW10 and T3N tetramer staining of HEK293 cells transfected with KIR3DL1*001 and a panel of KIR3DL1*001 interface residue mutants, normalized to TW10 tetramer binding to KIR3DL1*001 (c) or to the respective tetramer binding of KIR3DL1*001 transfectants (d). All results for c and d represent three independent experiments and are shown as mean and s.e.m. WT, wild-type.