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Fig. 2 | BMC Bioinformatics

Fig. 2

From: Structural prediction of the interaction of the tumor suppressor p27KIP1 with cyclin A/CDK2 identifies a novel catalytically relevant determinant

Fig. 2

Schematic visualization of p27KIP1 and structural model of the cyclin A/CDK2/p27KIP1 peptide (amino acids 180–194) complex. a Schematic representation of the domain organization of p27KIP1. The N-terminal segment (NTS, residues 1–28), the N-terminal kinase inhibitory domain (KID, residues 28–90), the C-terminal region (CT, residues 91–198), and the nuclear localization sequence (NLS, residues 152–169) are indicated. The known phosphorylation sites observed in p27KIP1 are also indicated [15]. The cyclin and CDK2 binding regions in KID are highlighted [21]. The available crystal structure data for p27KIP1 are highlighted by black bars (PDB ID: 1JSU (residues 25–93) [21] and 2AST (residues 181–190) [29]). The C-terminal binding region (residues 180–194), for which a structural model was constructed, is indicated by a dashed box. b The overall structure is shown in cartoon representation. CDK2, cyclin A, and the peptide substrate (amino acids 180–194 of p27KIP1) are colored in blue, orange, and green, respectively. The model contains ATP. c Close-up view of the binding interface between p27KIP1 and cyclin A/CDK2. Hydrogen bonds are highlighted in black dashed lines. d Sequence alignment showing the conservation of E42 in CDK2 compared with other CDKs. The sequence alignment was obtained using the Clustal Omega webserver [42]. Identical and structurally similar residues are indicated in red and green, respectively

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