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. 2017 May 4;7:85. doi: 10.3389/fonc.2017.00085

Figure 1.

Figure 1

KEAP1 and NRF2. (A) Two KEAP1 molecules and one NRF2 form a trimer through the DC domain in KEAP1 and the DLG and ETGE motifs within the N-terminal Neh2 domain of NRF2. This two-site binding of NRF2 and KEAP1 has been shown to be the molecular basis of electrophile-induced NRF2 accumulation. (B) The ratio of KEAP1:NRF2 binding. KEAP1 is unable to bind a large amount of NRF2.