Figure 5.

Model of CK1α (orange) with crystal structure of p53 transactivation domain (green) and ATP molecule (purple). a: Catalytic base Asp 136 in catalytic loop of kinase is coloured in cyan. p53 transactivation domain coloured in green consists of phosphoacceptor serine and the substrate constraint residue glutamic acid shown in stick representation. Substrate interacting residues arginine 214, lysine 260 and glycine 251 are shown in magenta and glycine loop is coloured in blue. b: Stereo figure showing the zoomed in view of the interaction between crystal structure of p53 transactivation domain and ck1α homology model. Other non-covalent interactions made between the kinase and the substrates are shown as discussed in Table 1.

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