Structural and biochemical characterization establishes a detailed understanding of KEAP1-CUL3 complex assembly

Abstract excerpt

KEAP1 promotes the ubiquitin-dependent degradation of NRF2 by assembling into a CUL3-dependent ubiquitin ligase complex. Oxidative and electrophilic stress inhibit KEAP1 allowing NRF2 to accumulate for transactivation of stress response genes. To date there are no structures of the KEAP1-CUL3 interaction nor binding data to show the contributions of different domains to their binding affinity. We determined a crys...

Topics

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• Binding Sites
• Imidazoles
• Intracellular Signaling Peptides and Proteins
• Kelch-Like ECH-Associated Protein 1
• Models, Molecular
• Molecular Conformation
• Protein Interaction Domains and Motifs
• Structure-Activity Relationship

Identifiers and source

Literature Corpus work

1b06502d-e78d-5ff9-9c2c-9c3918a09a58

DOI

10.1101/2023.02.15.528651