Figure 7
Figure 7. The D0 domains of KIR3DL2, KIR3DL1, KIR3DS1, and KIR2DL4 are involved in ODN recognition. (A) Each graph represents the ODN-binding capability of the full-length ectodomain of the reported KIRs and of their indicated extracellular domains. The starting and ending amino acids composing the indicated domains are listed in supplemental Table 2. Experimental conditions and data representations are described in Figure 6A. Results are reported as medians of 3 to 8 independent experiments, each performed in duplicate. IQRs are indicated. (B) KIR molecules and their domains were analyzed as titrations for the capability to bind ODN C. Experiments were performed and elaborated as described in Figure 6A. Data are represented as medians and IQRs of 4 independent experiments.

The D0 domains of KIR3DL2, KIR3DL1, KIR3DS1, and KIR2DL4 are involved in ODN recognition. (A) Each graph represents the ODN-binding capability of the full-length ectodomain of the reported KIRs and of their indicated extracellular domains. The starting and ending amino acids composing the indicated domains are listed in supplemental Table 2. Experimental conditions and data representations are described in Figure 6A. Results are reported as medians of 3 to 8 independent experiments, each performed in duplicate. IQRs are indicated. (B) KIR molecules and their domains were analyzed as titrations for the capability to bind ODN C. Experiments were performed and elaborated as described in Figure 6A. Data are represented as medians and IQRs of 4 independent experiments.

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