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Modeled complex of p27 residues 25–49 (green carbons) with Cyclin D1 (2W96) overlayed with SAKRNLFGM. The P35 and V36 interacting site on cyclin D1 is the region shown to provide a more extensive hydrophobic pocket than in the cyclin A2 context and which was exploited by methionine substitution (Met is the C-terminal residue in the p27 peptide colored with orange carbon atoms).
