Fig. 1
From: A state-of-the-art review on the NRF2 in Hepatitis virus-associated liver cancer
Major structures and functions of the Nrf2 (a) and Keap1 (b) domains are shown on a schematic diagram. 605 amino acids comprise the protein Nrf2, and its stability and transcriptional activity are regulated by seven functional domains called Nrf2-ECH homology (Neh) 1-7. Keap1, the primary intracellular regulator of Nrf2, is a 624-amino-acid protein composed of five domains: an N-terminal domain (NTD), a broad complex, tramtrack and bric-a-brac (BTB) domain, an intervening region (IVR), a double-glycine repeats (DGR) domain, and a C-terminal domain (CTD). Each of these domains plays a critical role in inhibiting Nrf2 activity. The DLG and ETGE motifs are significant for Keap1's binding to the N-terminal Neh2 domain of Nrf2. In response to oxidative stresses, the DLG motif in Nrf2 is uncoupled from the DGR domain in Keap1, protecting the protein from ubiquitination and degradation [20,21,22]