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. 2020 Sep 29;33(13):966–997. doi: 10.1089/ars.2020.8024

FIG. 1.

FIG. 1.

Schematic representation of the domain structure of NRF2 and KEAP1 proteins. (A) NRF2 comprises seven domains (Neh1–7). The Neh1 is responsible for DNA binding and dimerization with small Maf proteins. The Neh2 domain contains DLG and ETGE motifs that interact with KEAP1. The Neh3, Neh4, and Neh5 domains are transactivation domains; the Neh6 domain regulates NRF2 stability, and the Neh7 domain is responsible for RXRα binding. (B) KEAP1 contains five domains: the amino terminal NTR, CTR, and three major domains, BTB, IVR, and Kelch/DGR domains. The BTB domain associates with Cul3 and mediates KEAP1 dimerization. The IVR domain contains cysteine residues and connects the BTB and Kelch/DGR domains. The Kelch/DGR domain maintains the interaction between KEAP1 and NRF2. BTB, Broad complex/Tramtrack/bric-a-brac; CTR, carboxy-terminal; DGR, double glycine repeats; IVR, intervening region; KEAP1, Kelch-like ECH-associated protein 1; Neh, NRF2-ECH homology; NFE2, nuclear factor erythroid 2; NRF2, NFE2-related factor 2; NTR, N-terminal region; RXRα, retinoid X receptor α. Color images are available online.