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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 5. KEAP1 domain architecture and structure.

Figure 5.

A) KEAP1 is comprised of three structural domains the BTB domain, the IVR domain, and the Kelch domain. The numbering shown is for the human protein. The assigned functions of each of the domains is shown above each domain. Human KEAP1 has 27 cysteines that can work as sensors. The most important cysteine sensors are also shown. For a detailed discussion of domain and cysteine function, see the text. B) The BTB domain of KEAP1 forms a functional dimer to bind to a single NRF2 protein. This dual binding mode is essential for physiologic function. (PDB ID 4CXI). C) The BTB domain bound to the N-terminus of CUL3. (PDB ID 5NLB). D) The unliganded Kelch domain of KEAP1. (PDB ID 5WFV).