Fig. 3: Co-crystal structure of 14-3-3β in complex with the ChREBP α2 peptide and stabilizer 3. | Nature Communications

Fig. 3: Co-crystal structure of 14-3-3β in complex with the ChREBP α2 peptide and stabilizer 3.

From: Structure-based evolution of a promiscuous inhibitor to a selective stabilizer of protein–protein interactions

Fig. 3

a Side view of the 14-3-3 dimer (white cartoon representation) bound by two ChREBP peptides (red cartoon) and two 3 molecules (blue sticks). b Top view displaying the antiparallel orientation of the ChREBP α helices in the 14-3-3 dimer. c Front view of one 14-3-3 monomer (white surface) bound by one ChREBP α-helix and 3. Final 2Fo–Fc electron density (blue mesh, contoured at 1.0σ) displayed for the ChREBP peptide and 3. The panel highlights the interactions 3 makes with 14-3-3 and ChREBP residues (relevant side chains are displayed in stick representation). Polar contacts are displayed as black dashed lines. d, e Detailed view of the composite pocket occupied by 3 created by ChREBP and 14-3-3 together, illustrating its interface-binding character. Both phenyl rings of 3 make hydrophobic contacts with side chains of both proteins, as observed for the phenylphosphonate with W127 of ChREBP, and the second phenyl with I120 of ChREBP and I219, L222, and L174 of 14-3-3. Residues of both protein partners that make up the binding pocket are represented as cartoon and sticks (d) or surface (e).

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