Figure 4
From: Structural investigation of nucleophosmin interaction with the tumor suppressor Fbw7γ
Molecular docking analysis of the Fbw7γ*-Nter-NPM1 interaction. The interaction between Fbw7γ* and Nter-NPM1 investigated through molecular docking analysis is shown. (a) Nter-NPM1 pentamer is represented in cartoon while the Fbw7γ* peptide is shown in sticks. (b) The Nter-NPM1 electrostatic surface is shown in a different orientation from a. The peptide, shown in sticks, adopts an extended conformation with its C-terminal end protruding into the central pentamer cavity. (c) A detail of the interaction played by Nter-NPM1 residue D36 with Fbw7γ* R47. (d) Nter-NPM1 residue is predicted to interact with both Fbw7γ* R48 and R52 residues. (e) Interaction between Nter-NPM1 E93 and Fbw7γ* K53. (f) Nter-NPM1 residue E37 is also predicted to interact with Fbw7γ* R47. (g) E121 residues from two different Nter-NPM1 monomers (the second one is shown in magenta) are predicted to interact with residue K51 and R52 residues.
