Fig. 7: Sequence conservation at CDC25A binding regions. | Nature Communications

Fig. 7: Sequence conservation at CDC25A binding regions.

From: Cryo-EM structure of the CDK2-cyclin A-CDC25A complex

Fig. 7

Sequence conservation is indicated in purple (darker shade = identical, lighter shade = similar, white = different) and selected residues directly involved in CDC25A binding are highlighted in red boxes. a Sequence conservation of CDK2 vs CDK1, 3, 4 and 6 around the GDSEID-αG helix motif. b Structural overlay of CDK2 (purple) with CDK4 (orange) and CDK6 (blue) showing changes in residue identity for Asp206, Phe213 and Arg217 at the GDSEID-αG helix motif (c) Sequence conservation of cyclin A vs cyclin B, E, D1 and D3 around the central helix (α3’) in the cyclin A C-CBF. d Structural overlay of cyclin A (salmon) with cyclin D1 (grey) and cyclin D3 (yellow), highlighting the changes in residues identity for Tyr269 and Gly272 in the C-CBF. e Sequence conservation of CDC25A vs CDC25 B and C at the C-terminal helix region. f Ribbon diagram of CDC25A coloured by sequence conservation. CDC25A residues Arg506, Ser513 and Lys514 highlighted on the C-terminal (α6) helix are non-conserved in CDC25C.

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