Fig. 3: Interactions of CDC25A with CDK2.
a–c Interactions of the CDK2 G-loop with the CDC25A active site. a Overlay of CDK2 (purple) with pT160CDK2-cyclin A crystal structure (PDB 1JST, grey), highlighting a change in G-loop conformation. The CDC25A CX5R loop is highlighted in yellow. b Electrostatic surface of the CDC25A active site, showing binding of CDK2 pTyr15. c Ribbon and density diagram (0.06 threshold) for the binding of CDK2 pTyr15 in the CDC25A active site. pTyr15 and the mutated catalytic cysteine residue (Cys431Ser) are labelled in a and c. d–f Interactions of the CDK2 activation segment with the CDC25A C-terminal helix (α6). d Ribbon diagram of the trimeric complex, highlighting the CDK2 activation segment (yellow). e Electrostatic surface of the CDK2 activation segment and CDC25A C-terminal helix. f Ribbon and density diagram (threshold 0.17) depicting binding of the CDK2 activation segment with the CDC25A C-terminal helix, which also binds cyclin A Tyr269 (salmon). g–i Interactions of the GDSEID motif with CDC25A. g Ribbon diagram highlighting the CDK2 GDSEID motif and αG helix (yellow). h Electrostatic profile of CDK2 GDSEID motif and (i) Ribbon and density diagram (threshold 0.14) for binding of the CDK2 GDSEID motif (purple) with the central helix of CDC25A (green).
