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. 2014 Mar 31;57(9):3835–3844. doi: 10.1021/jm500165n

Table 3. Relative Binding Affinities of Ligands to the Wild-Type C1b Domain of PKCδ and to Mutated Versions Incorporating One or More of the Residues of PKCζ/ι Responsible for Its Loss of Ligand Binding Activity.

    Kd or Ki relative to that for PDBu binding to the wtδC1ba
compd Kd, nM,a wtδC1B N7R S10R P11R L20R N7R/P11R N7R/L20R N7R/S10R/P11R N7R/S10R/L20R
PDBu (0.23) 5.13 1.39 5.17 34.7 147 2090 85.2 5900
1-E (2.95) 1.12 0.79 3.53 4.75 12.5 81.0 21.3 224
2-E (2.46) 1.01 0.85 0.94 7.87 NTb NTb NTb NTb
3-E (2.95) 0.67 0.40 0.50 3.20 NTb NTb NTb NTb
4-E (2102) 0.30 0.40 0.20 1.34 2.47 21.8 NTb NTb
5-E (560) 1.41 1.45 1.27 12.4 6.79 209 NTb NTb
5-Z (865) 0.55 0.57 1.09 3.25 3.25 60.0 NTb NTb
6-E (1206) 1.44 1.46 2.79 4.57 13.2 87.0 NTb NTb
7-E (1070) 0.82 0.62 0.93 5.74 3.49 78.0 NTb NTb
8-E (300) 0.94 1.56 0.33 5.33 NTb NTb NTb NTb
9-E (96) 1.25 0.98 1.25 7.70 NTb NTb NTb NTb
10-E (1) 0.90 1.50 1.70 17.3 NTb NTb NTb NTb
11-E (0.5) 1.20 1.20 2.00 17.6 NTb NTb NTb NTb
12-E (0.6) 1.17 1.00 2.00 17.5 NTb NTb NTb NTb
13-E (777) 1.04 1.44 2.61 1.04 30.7 9.83 60.5 10.1
a

Data are derived from Table 2.

b

NT, not tested.