Table 1

List of interactions between human casein kinase 1α and substrate p53 tumour suppressor transactivation domain
Residues in the crystal structure of p53 transactivation domain Substrate interacting residues of human casein kinase 1α Nature of interaction
E17 R214, K260, G251 Ionic interaction
T18 T212 Hydrogen bonding
F19 K260 Cation-π interaction
D21 K138 Ionic interaction
K24 D136 Ionic interaction
L25 F28 Hydrophobic interaction
P27 A52, P55 Hydrophobic interaction
E28 R135 Ionic interaction

Interactions observed in the modelled complex of p53 tumour suppressor transactivation domain [21] bound to CK1α model as shown in Figure 5.

Sudha et al.

Sudha et al. BMC Structural Biology 2012 12:28   doi:10.1186/1472-6807-12-28

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