Fig. 4: A predicted model of the interaction between PAK4 and CDK2.
From: PAK4 phosphorylates cyclin-dependent kinase 2 to promote the G1/S transition during adipogenesis
a The binding interaction between PAK4 and CDK2 was predicted through computational modeling. The secondary structures of PAK4 and CDK2 are shown in pale-green and light-blue ribbons, respectively. The two residues involved in phosphorylation, that is, PAK4-pS474 and CDK2-S106, are depicted as spheres. The ATP-Mg2+ molecule is displayed as sticks at the ATP-binding site. b The molecular surfaces of PAK4 and CDK2 are displayed with electrostatic potential. The binding interface, outlined by a black box, illustrates the complementary electrostatic interactions between PAK4 (left) and CDK2 (right), with regions of positive charge in blue and negative charge in red. The model suggests that PAK4-mediated phosphorylation of CDK2 at the S106 residue is structurally feasible.
