Fig 1: Schematic showing the domain architecture of KEAP1 and CUL3 and predicted model for their interaction. KEAP1 is shown as a homodimer in red and blue. Substrate degrons (purple) are shown bound to the Kelch domains. The CUL3 (light brown) C-terminal domain (CTD) is bound to RBX1 (claret). The CUL3 N-terminal domain (NTD) and 22 residue N-terminal extension (N22) are predicted to bind to the KEAP1 BTB and 3-box domains (model based on the previously determined structure of a KLHL11-CUL3 complex [29]). The BTB domain was first identified as a conserved motif in the Drosophila proteins bric-à-brac, tramtrack and broad complex (reviewed in Ref. [34]). Likewise, the Kelch repeat domain was first identified in the Drosophila Kelch protein (reviewed in Ref. [35]). The BACK domain (for BTB and C-terminal Kelch) is also known as the intervening region (IVR) in KEAP1 and includes the 3-box motif at it N-terminus [36].
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