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. Author manuscript; available in PMC: 2021 Jun 1.
Published in final edited form as: Nat Prod Rep. 2020 May 13;37(6):797–826. doi: 10.1039/c9np00061e

Figure 4. The KEAP1 Kelch domain bound to ETGE and DLG containing peptides.

Figure 4.

A) and B) The ETGE motif binds to a series of positively charged amino acids in the KEAP1 Kelch domain. The ETGE forms a loop in the binding pose. Two views are shown: from the top A) and the side B). (PDB ID 5WFV). C) and D) The DLG containing peptide shows a pose like the ETGE, but shows fewer contacts, explaining the decreased affinity. The rest of the peptide forms an alpha-helical structure, but this is not known to be physiological or significant due to lack of larger structural data. Two views are shown: from the top C) and the side D). (PDB ID 3WN7).