Related Experiment Video
Updated: Jul 5, 2026

In Vitro Selection of Engineered Transcriptional Repressors for Targeted Epigenetic Silencing
Published on: May 5, 2023
Structural insights into the similar modes of Nrf2 transcription factor recognition by the cytoplasmic repressor
Balasundaram Padmanabhan1, Kit I Tong, Akira Kobayashi
1Genomic Sciences Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Abstract:
The cytoplasmic repressor Keap1 regulates the function of transcription factor Nrf2 which plays critical roles in oxidative and xenobiotic stresses. The Neh2 domain of Nrf2 interacts with Keap1 at the bottom region of the Kelch/beta-propeller domain which is formed by double-glycine repeat and C-terminal region domains (Keap1-DC). The structure of Keap1-DC complexed with an Nrf2 peptide containing a conserved DLG motif has been determined at 1.9 A resolution. The Keap1-bound DLG peptide possesses a hairpin conformation, and it binds to the Keap1 protein at the bottom region of the beta-propeller domain. The intermolecular interaction occurs through their complementary electrostatic interactions. Comparison of the present structure with the recently reported Keap1-DC complex structure suggests that the DLG and ETGE motifs of Neh2 in Nrf2 bind to Keap1 in a similar manner but with different binding potencies.
Related Concept Videos
Co-activators and Co-repressors
Co-activators and Co-repressors
Regulation of Nuclear Protein Sorting
Regulation of the Unfolded Protein Response
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
