Figure 2
From: Cryo-EM structure of SKP1-SKP2-CKS1 in complex with CDK2-cyclin A-p27KIP1
Interaction of CKS1 with CDK2, SKP2 and p27. (a,b) Interface between CKS1 (pink) and CDK2 (blue). (a) Electrostatic surface potential of CDK2 showing the narrow groove in which CKS1 residues Met58-Glu63 bind. (b) Ribbon diagram of CDK2-CKS1 interface highlighting the CDK2 residues that form the surface groove (Lys237, Phe240, Phe213, Asp235, Leu175) and density (at 8.8σ, threshold 0.337) for the interacting residues of CKS1, notably His60 and Pro62. (c,d) Interface between SKP2 (grey) and CKS1 (pink). (c) Electrostatic surface potential of CKS1 depicting the hydrophobic pocket in which SKP2 Phe393 binds (d) Ribbon diagram of SKP2-CKS1 interface showing density (at 8.8σ, threshold 0.406) for the binding of SKP2 Phe393 and His392 (e,f) Binding of p27 (yellow) with CKS1 (pink). (e) Electrostatic surface potential of CKS1 revealing the binding of p27 phosphorylated Thr187 in a positively charged pocket and Pro188 in a hydrophobic groove (f) Ribbon diagram of p27 showing density (at 8.8σ, threshold 0.346) for the phosphorylated Thr187 protruding into CKS1 whilst p27 Pro188 stacks over CSK1 Tyr8 and is wedged by CKS1 Gln5 and Gln49.
