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Fig. 12 | Molecular Cancer

Fig. 12

From: PROTAC’ing oncoproteins: targeted protein degradation for cancer therapy

Fig. 12

Crystal structure of the VHL-ElonginC-ElonginB (VCB)-GSK215-FAK ternary complex (PDB 7PI4). The VHL-FAK neo-PPI interface maps to 2661 Å2, the largest of any reported PROTAC ternary complex. The VHL ligand is buried within a pocket defined by both the surface of VHL and FAK. Hydrogen bonding interactions with VHL residues Y98, R107, H110, and S111 are shown. The linker carbonyl forms water-mediated hydrogen bonds with VHL residues N67 and R69. Additional hydrogen bonds with FAK residues C502 and D564 are shown. Image created using Schrödinger Bioluminate with PDB 7PI4. VHL is depicted in cyan and FAK in brownish orange

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