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. Author manuscript; available in PMC: 2020 Jun 1.
Published in final edited form as: Curr Opin Chem Biol. 2019 Mar 23;50:55–65. doi: 10.1016/j.cbpa.2019.02.012

Figure 3. Examples of p97 small molecule inhibitors.

Figure 3.

The center cartoon shows the domain structure of p97, with arrows pointing to the binding sites for allosteric and ATP-competitive inhibitors. Each monomer in the p97 hexamer has three folded domains: the N-terminal PPI domain (purple), the D1 ATPase domain (orange), and the D2 ATPase domain (blue). Competitive inhibitors ML240 and CB5083 (left panel) bind at the ATP-binding pocket of p97 D2 domain (light blue). Inhibitors UPCDC30245 and NMS-873 (right panel) bind at allosteric sites in the D2 ATPase domain, near the D1-D2 linker region (red). The binding site for allosteric inhibitors has been defined by cross-linking, resistant mutants, and cryo-EM. See references in the main text.