Table 1 KIR2DL2 and KIR2DL3 binding to HLA-C*07:02-RL9-P7/P8 mutant peptide panel.

From: Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C

Peptide

KIR2DL2

KIR2DL3

  

KD (μM)

SD (±μM)

KD (μM)

SD (±μM)

p value

q value

WT

4.9

0.3

4.2

0.3

0.31

0.39

P7E

n.d.

n.d.

n.d.

n.d.

n.d.

n.d.

P7F

14.4

0.5

12.4

1.6

0.23

0.37

P7G

27.9

2.1

21.0

1.6

0.07

0.27

P7A

27.7

3.3

20.6

0.7

0.10

0.27

P7N

29.7

5.7

21.5

1.5

0.19

0.35

P7R

17.6

0.9

14.4

3.0

0.28

0.39

P8E

n.d.

n.d.

n.d.

n.d.

n.d.

n.d.

P8F

6.5

0.4

5.1

0.4

0.07

0.27

P8G

18.9

0.7

11.7

0.8

0.01

0.12

P8V

7.5

1.0

5.6

0.6

0.15

0.33

P8N

20.0

5.8

19.9

2.0

0.99

0.99

P8R

23.9

1.5

22.8

1.5

0.54

0.60

  1. WT wild-type RL9 peptide (RYRPGTVAL), n.d. not determined, KD equilibrium dissociation constant, SD standard deviation of calculated KD value.
  2. KD values calculated via steady-state analysis of n = 2 injections of serially diluted KIR2DL analyte described in full in Supplementary Fig. 6. Representative values of n = 2 independent experiments are shown. Differences between KIR2DL2 and KIR2DL3 binding to each ligand was assessed by multiple unpaired two-sample t-test using a false discovery rate (FDR) approach (two-stage step-up method). p and q values for each comparison are shown. With a desired FDR (Q) of 1%, no discoveries were observed.
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