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. 2021 Jun 2;64(12):8423–8436. doi: 10.1021/acs.jmedchem.1c00401

Figure 1.

Figure 1

Exploring the p65/14-3-3 interface with imine forming fragments. (A) Overview of the composite binding pocket of 14-3-3 and the p65_45 peptide (PDB: 6QHL).38 (B) Crystal structure of the NF-κB subunit p65 (PDB: 1IKN,39 IκBα and p50 hidden for clarity) with known phosphorylated serine residues Ser281 and Ser45 labeled. (C) Interface of the ternary complex of 1/p65_45/14-3-3 (PDB: 6YOW).25 Indicated are three subpockets (the roof of 14-3-3, the FC-binding pocket, and the deep binding pocket), which can be exploited by fragment extension. Shown are 14-3-3 (white sticks, surface and cartoon), p65_45 peptide (red sticks), and fragment 1 (cyan sticks). (D) Fragment hits based on X-crystallography screening with benzaldehyde binding to Lys122 of 14-3-3.