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. 2022 Aug 29;11(9):1685. doi: 10.3390/antiox11091685

Figure 2.

Figure 2

Structures of Nrf2 and Keap1. (A) The Nrf2 protein comprises seven Neh domains, known as Neh1–Neh7. The Neh1 domain is responsible for DNA binding and dimerization with the sMaf proteins; the Neh2 domain mediates the interaction with Keap1 through the ETGE motifs and gathers a ubiquitin ligase to the fusion protein through the DLG element; the Neh3, Neh4, and Neh5 domains are transactivation domains; the Neh6 domain regulates Nrf2 stability; and the Neh7 domain binds with RXRα to weaken the cytoprotective effect of Nrf2. (B) Keap1 possesses three functional domains. The BTB domain mediates Keap1 homodimerization and associates with Cul3; the DC directly associates with Nrf2 Neh2 domain; IVR domain contains critical cysteine residues and connects the BTB domain with DC domain.