Cited by 627Genomics, phytochemicals, and oxidative stressUbiquitin and proteasome pathwaysRedox biology and oxidative stress

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Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

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Lo, Shih‐Ching, Li, Xuchu, Henzl, Michael T, Beamer, Lesa J, Hannink, Mark·2006·The EMBO Journal

DOI 10.1038/sj.emboj.7601243PMC PMC1538563

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Abstract

Keap1 is a BTB-Kelch substrate adaptor protein that regulates steady-state levels of Nrf2, a bZIP transcription factor, in response to oxidative stress. We have determined the structure of the Kelch domain of Keap1 bound to a 16-mer peptide from Nrf2 containing a highly conserved DxETGE motif. The Nrf2 peptide contains two short antiparallel beta-strands connected by two overlapping type I beta-turns stabilized by the aspartate and threonine residues. The beta-turn region fits into a binding pocket on the top face of the Kelch domain and the glutamate residues form multiple hydrogen bonds with highly conserved residues in Keap1. Mutagenesis experiments confirmed the role of individual amino acids for binding of Nrf2 to Keap1 and for Keap1-mediated repression of Nrf2-dependent gene expression. Our results provide a detailed picture of how a BTB-Kelch substrate adaptor protein binds to its cognate substrate and will enable the rational design of novel chemopreventive agents.

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“The Kelch domain of Keap1 is combined with the Neh2 domain of Nrf2 [45,46].”
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The Marburg Virus VP24 Protein Interacts with Keap1 to Activate the Cytoprotective Antioxidant Response Pathway
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“The mutation to alanine of Keap1 Kelch domain residue R415 disrupts interaction with Nrf2 (Lo et al., 2006).”
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“The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses”
BackgroundMethodInfluential
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“Mutagenesis experiments have provided strong evidences that individual substitution of these two amino acids in KEAP1 impaired its ability to bind with Nrf2 and to mediate repression of Nrf2-dependent gene expression [56, 57].”
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“DxETGE motif would position these residues for ubiquitin transfer and then facilitate the ubiquitination and degradation of Nrf2 [27].”
Background
Molecular Evolution of Keap1
Li, L., Kobayashi, M., Kaneko, H., Nakajima‐Takagi, Y., Nakayama, Y., & Yamamoto, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708702200 · Cited by 111
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“Nrf2 is negatively regulated by Kelchlike ECH-associated protein 1 (Keap1) [11].”
Background
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“In crystal structures of a Nrf2 peptide bound to the Kelch domain [55], Glu 79 and Glu 82 of the ETGE motif form ionic interactions with Arg 415 and 483 of Keap1 [55].”
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Angiotensin II signaling via protein kinase C phosphorylates Kelch-like 3, preventing WNK4 degradation
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“This site lies in a “d–a” loop between successive blades of the Kelch propeller; these loops are involved in substrate binding (25).”
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“The available crystal structures 18,80 of the human Keap1 Kelch domain were also used for an in silico fragment-based approach to discover 1,4-diaryl-1,2,3-triazole inhibitors of the Keap1-Nrf2 PPI.”
BackgroundMethodInfluential
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“The FP assay of the N-acetylated 9mer Nrf2 peptides showed similar binding affinities to the longer peptides with Keap1.”
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“In addition, Keap1 mutant H436A demonstrates dramatically decreased affinity for an Neh2-derived peptide and shows no detectable ability to repress Nrf2 in a reporter assay (56).”
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“Thus, occupying the Kelch structural domain of Keap1, which competitively binds to Nrf2, can facilitate Nrf2 entry into the nucleus and initiate downstream antioxidant enzymes [45].”
Background
Nrf2 deficiency potentiates methamphetamine‐induced dopaminergic axonal damage and gliosis in the striatum
Granado, N., Lastres‐Becker, I., Ares‐Santos, S., Oliva, I., Martín, E. D., Cuadrado, A., & Moratalla, R. (2011) · Glia · doi:10.1002/glia.21229 · Cited by 93
“Nrf2 has a very short half-life because of its interaction with the BTB-Kelch protein Keap1, which promotes Nrf2 degradation by the proteasome (Lo et al., 2006).”
Background
Pterostilbene-mediated Nrf2 activation: Mechanistic insights on Keap1:Nrf2 interface
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“KEAP1 NRF2 [DNS]x[DES][TNS ]GE 2FLU [76] Compound 7”
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“[55,56].”
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Background
Targeting NRF2 to treat cancer
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Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction with improved binding and cellular activity
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Cyclic peptide structure prediction and design using AlphaFold2
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“Keap1 is the receptor for a Cul3 ‐ dependent ubiquitin ligase complex that recognizes and targets the transcription activator Nrf2 for degradation 42 .”
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“Several ETGE-containing peptides have been reported to bind Keap1 Kelch domain with varying affinity, and these include the 16mer Nrf2 peptide (residues 69–84), 14mer Nrf2 peptide (residues 74–87), and 10mer Nrf2 peptide (residues 76–85) (38).”
BackgroundMethodResultInfluentialSelf-citation
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“The 24 candidates bind with the special amino acids on Keap1, such as Ser363, Ser508, Ser555 and Ser602, which have been reported to be the key amino acids in the structure of the Keap1−Nrf2 interface (Lo et al., 2014).”
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S‐Glutathionylation of Keap1: a new role for glutathioneS‐transferase pi in neuronal protection
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Discovery of a head-to-tail cyclic peptide as the Keap1-Nrf2 protein-protein interaction inhibitor with high cell potency
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“Each blade is a twisted β-sheet composed of four antiparallel β-strands (A–D): strand A is positioned in line with the central channel and runs almost parallel with the six-fold axis of the propeller, while strands B–D progressively acquire more distance from the central axis and exhibit more twist until almost comple…”
Background
The anti-inflammatory activity of Phellinus linteus (Berk. & M.A. Curt.) is mediated through the PKCδ/Nrf2/ARE signaling to up-regulation of heme oxygenase-1
Kim, B.-C., Jeon, W.-K., Hong, H.-Y., Jeon, K. B., Hahn, J.-H., Kim, Y., Numazawa, S., Yosida, T., Park, E., & Lim, C. (2007) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2007.05.032 · Cited by 73
Defining the functional targets of cap'n'collar transcription factors NRF1, NRF2, and NRF3
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“We introduced a mutation (T80D) in the Neh1 domain of NRF2, which has been reported to inhibit its interactions with KEAP1 and to promote constitutive transcriptional activation [25].”
Background
Investigation of Molecular Details of Keap1-Nrf2 Inhibitors Using Molecular Dynamics and Umbrella Sampling Techniques
Londhe, A. M., Gadhe, C. G., Lim, S. M., & Pae, A. N. (2019) · Molecules · doi:10.3390/molecules24224085 · Cited by 72
“Nrf2 is a precursor for several defensive enzymes and antioxidants used against xenobiotics [6,7].”
Background
Current strategies and progress for targeting the “undruggable” transcription factors
Zhuang, J., Liu, Q., Wu, D., & Tie, L. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00852-9 · Cited by 77
“With the elucidation of the co-crystal structures of Keap1 and Nrf2 peptides, a large number of Keap1-Nrf2 inhibitors targeting their PPI have been reported, including small molecules and peptides [76, 77].”
Background
Withaferin A induces heme oxygenase (HO-1) expression in endothelial cells via activation of the Keap1/Nrf2 pathway
Heyninck, K., Sabbe, L., Chirumamilla, C. S., Szic, K. S. V., der Veken, P. V., Lemmens, K. J. A., Lahtela-Kakkonen, M. K., Naulaerts, S., de Beeck, K. O., Laukens, K., et al. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.03.026 · Cited by 69
The emerging role for Cullin 4 family of E3 ligases in tumorigenesis
Cheng, J., Guo, J., North, B. J., Tao, K., Zhou, P., & Wei, W. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.11.007 · Cited by 69
Natural products as non-covalent and covalent modulators of the KEAP1/NRF2 pathway exerting antioxidant effects
Culletta, G., Buttari, B., Arese, M., Brogi, S., Almerico, A. M., Saso, L., & Tutone, M. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116355 · Cited by 73
Interaction with CREB binding protein modulates the activities of Nrf2 and NF-κB in cystic fibrosis airway epithelial cells
Ziady, A. G., Sokolow, A. G., Shank, S. L., Corey, D. A., Myers, R., Plafker, S. M., & Kelley, T. J. (2012) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00156.2011 · Cited by 71
Cullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to fine-tune DNA-end resection
Ferretti, L. P., Himmels, S.-F., Trenner, A., Walker, C., von Aesch, C., Eggenschwiler, A., Murina, O., Enchev, R. I., Peter, M., Freire, R., et al. (2016) · Nature Communications · doi:10.1038/ncomms12628 · Cited by 70
“Importantly, mutation of these residues in Keap1 disrupted its ability to bind Nrf2 and repress Nrf2-dependent transcription 25,26 .”
Sunflower seed-derived bioactive peptides show antioxidant and anti-inflammatory activity: From in silico simulation to the animal model
Tonolo, F., Coletta, S., Fiorese, F., Grinzato, A., Albanesi, M., Folda, A., Ferro, S., Mario, A. D., Piazza, I., Mammucari, C., et al. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.138124 · Cited by 66
The Molecular Genetics of Gordon Syndrome
Mabillard, H. R., & Sayer, J. A. (2019) · Genes · doi:10.3390/genes10120986 · Cited by 68
“As many of these subjects had de novo CUL3 mutations, impairment of reproductive fitness is likely [97].”
BackgroundInfluential
Emerging Substrate Proteins of Kelch-like ECH Associated Protein 1 (Keap1) and Potential Challenges for the Development of Small-Molecule Inhibitors of the Keap1-Nuclear Factor Erythroid 2‑Related Factor 2 (Nrf2) Protein–Protein Interaction
Zhang, Y., Shi, Z., Zhou, Y., Xiao, Q., Wang, H., & Peng, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01865 · Cited by 67
Identification and molecular mechanism of novel antioxidant peptides from tiger nut (Cyperus esculentus L.)
Quan, Y., Ren, H., Liu, S., Zhao, X., & Hao, J. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.105738 · Cited by 66
p62-Dependent Phase Separation of Patient-Derived KEAP1 Mutations and NRF2
Cloer, E. W., Siesser, P. F., Cousins, E. M., Goldfarb, D., Mowrey, D. D., Harrison, J. S., Weir, S., Dokholyan, N. V., & Major, M. B. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00644-17 · Cited by 69
Biological and therapeutic activities of thymoquinone: Focus on the Nrf2 signaling pathway
Talebi, M., Talebi, M., Farkhondeh, T., & Samarghandian, S. (2020) · Phytotherapy Research · doi:10.1002/ptr.6905 · Cited by 68
Targeting NRF2–KEAP1 axis by Omega-3 fatty acids and their derivatives: Emerging opportunities against aging and diseases
Davinelli, S., Medoro, A., Intrieri, M., Saso, L., Scapagnini, G., & Kang, J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.11.017 · Cited by 72
Updated Research and Applications of Small Molecule Inhibitors of Keap1-Nrf2 Protein-Protein Interaction: a Review
Zhuang, C., Miao, Z., Sheng, C., & Zhang, W. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217104648 · Cited by 67
Activation of anti-oxidant Nrf2 signaling by enone analogues of curcumin
Deck, L. M., Hunsaker, L. A., Jagt, T. A. V., Whalen, L. J., Royer, R. E., & Jagt, D. L. V. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.11.048 · Cited by 65
Functional Aspects of Redox Control During Neuroinflammation
Rosales‐Corral, S., Reiter, R. J., Tan, D., Ortiz, G. G., & López-Armas, G. D. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2629 · Cited by 66
“Keap1 also has an intervening region (IVR) sequence, outside the BTB domain, responsible for the association between Keap1 and the Cullin-based E3-ligase (Cul3), a subunit of the ubiquitin E3 ligase complex, and transfers ubiquitin to Nrf2 protein (153).”
Influential
CRISPR/Cas9 genome-wide screening identifies KEAP1 as a sorafenib, lenvatinib, and regorafenib sensitivity gene in hepatocellular carcinoma
Zheng, A., Chevalier, N., Calderoni, M., Dubuis, G., Dormond, O., Ziros, P. G., Sykiotis, G., & Widmann, C. (2019) · OncoTarget · doi:10.18632/oncotarget.27361 · Cited by 55
“In our screen, all six sgRNAs targeted the Kelch domain of KEAP1, which is responsible for the binding to Nrf2 [13].”
Background
Growth, digestive and absorptive capacity and antioxidant status in intestine and hepatopancreas of sub-adult grass carp Ctenopharyngodonidella fed graded levels of dietary threonine
Hong, Y., Jiang, W., Kuang, S., Hu, K., Tang, L. Y., Liu, Y., Jiang, J., Zhang, Y., Zhou, X., & Feng, L. (2015) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-015-0032-1 · Cited by 61
“Furthermore, the conserved threonine residue was essential for the structure stabilization of Nrf2 in HEK-293 T cells [77].”
Background
Structural and mechanistic insights into the Keap1-Nrf2 system as a route to drug discovery
Madden, S. K., & Itzhaki, L. S. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140405 · Cited by 62
NRF2 in human neoplasm: Cancer biology and potential therapeutic target
Liu, Y., Lang, F., & Yang, C. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107664 · Cited by 60
Direct Keap1-kelch inhibitors as potential drug candidates for oxidative stress-orchestrated diseases: A review on In silico perspective
Boyenle, I. D., Divine, U. C., Adeyemi, R. O., Ayinde, K. S., Olaoba, O. T., Apu, C., Du, L., Lü, Q., Yin, X., & Adelusi, T. I. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105577 · Cited by 59
Novel protein–protein interaction inhibitor of Nrf2–Keap1 discovered by structure-based virtual screening
Sun, H.-P., Jiang, Z., Zhang, M.-Y., Lu, M., Yang, T., Pan, Y., Huang, H., Zhang, X., & You, Q. (2013) · MedChemComm · doi:10.1039/c3md00240c · Cited by 59
Perillyl alcohol attenuates rheumatoid arthritis via regulating TLR4/NF-κB and Keap1/Nrf2 signaling pathways: A comprehensive study onin-vitro and in-vivo experimental models
Puppala, E. R., Jain, S., Saha, P., Rachamalla, M., Syamprasad, N. P., Yalamarthi, S. S., Abubakar, M., Chaudhary, A., Chamundeswari, D., Murty, U. S. N., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.153926 · Cited by 59
Formation, signaling functions, and metabolisms of nitrated cyclic nucleotide
Sawa, T., Ihara, H., Ida, T., Fujii, S., Nishida, M., & Akaike, T. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.04.004 · Cited by 58
Adaptation of the master antioxidant response connects metabolism, lifespan and feather development pathways in birds
Castiglione, G. M., Xu, Z., Zhou, L., & Duh, E. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16129-4 · Cited by 63
Thioredoxin Signaling Pathways in Cancer
Zhang, J., Li, X., Zhao, Z., Cai, W., & Fang, J. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0074 · Cited by 60
“Keap1 in mammalian cells is a highly cysteine-rich protein, and bridges the cullin3 E3 ubiquitin ligase and Nrf2, leading to the ubiquitination of Nrf2 and subsequent proteasome degradation of Nrf2 (Lo et al, 2006) (Fig.”
Self-citation
CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases
Wang, P., Song, J., & Ye, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_13 · Cited by 53
Virtual Screening of Peptide Libraries: The Search for Peptide-Based Therapeutics Using Computational Tools
Vincenzi, M., Mercurio, F. A., & Leone, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031798 · Cited by 63
“…ID: 6WYD [136]) (Figure 1a), XO in complex with quercetin (PDB ID: 3NVY [137]) (Figure 1b), Keap1 in complex with an Nrf2 peptide (PDB ID: 2FLU [138]) and p47phox in complex with a p22phox peptide (PDB ID: 1WLP [139]) were retrieved from the PDB and the regions of interaction with their…”
MethodInfluential
Induction of Heme Oxygenase I (HMOX1) by HPP-4382: A Novel Modulator of Bach1 Activity
Attucks, O. C., Jasmer, K. J., Hannink, M., Kassis, J. N., Zhong, Z., Gupta, S., Victory, S. F., Güzel, M., Rao, P. D., Andrews, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101044 · Cited by 55
Self-citation
Adaptive HNE-Nrf2-HO-1 pathway against oxidative stress is associated with acute gastric mucosal lesions
Ueda, K., Ueyama, T., Yoshida, K., Kimura, H. M., Ito, T., Shimizu, Y., Oka, M., Tsuruo, Y., & Ichinose, M. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00204.2007 · Cited by 56
Design and Synthesis of Irreversible Analogues of Bardoxolone Methyl for the Identification of Pharmacologically Relevant Targets and Interaction Sites
Wong, M. H. L., Bryan, H. K., Copple, I. M., Jenkins, R. E., Chiu, P. H., Bibby, J., Berry, N. G., Kitteringham, N. R., Goldring, C. E., O’Neill, P. M., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01292 · Cited by 56
Replacement of a Naphthalene Scaffold in Kelch-like ECH-Associated Protein 1 (KEAP1)/Nuclear Factor (Erythroid-derived 2)-like 2 (NRF2) Inhibitors
Richardson, B. G., Jain, A. D., Potteti, H. R., Lazzara, P. R., David, B. P., Tamatam, C. R., Choma, E., Skowron, K. J., Dye, K., Siddiqui, Z., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01133 · Cited by 57
Effect of Tacrine‐3‐caffeic Acid, A Novel Multifunctional Anti‐Alzheimer's Dimer, Against Oxidative‐Stress‐Induced Cell Death in HT 22 Hippocampal Neurons: Involvement of Nrf2/ HO ‐1 Pathway
Chao, X., Chen, Z., Liu, A., He, X., Wang, S., Wang, Y., Liu, P., Ramassamy, C., Mak, S., Cui, W., et al. (2014) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12286 · Cited by 55
“The disassociation of Nrf2 from Keap1 may be through the direct modification of reactive cysteine residues in Keap1 by endogenous products of OS or reactive chemicals [12,62,63].”
Background
Giant axonal neuropathy
Yang, Y., Allen, E., Ding, J., & Wang, W. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6396-4 · Cited by 55
Emerging Screening Approaches in the Development of Nrf2–Keap1 Protein–Protein Interaction Inhibitors
Leung, C., Zhang, J.-T., Yang, G., Liu, H., Han, Q., & Ma, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184445 · Cited by 54
“Human Keap1 has five domains: the N-terminal region (NTR), the broad-complex, tramtrack and bric a brac (BTB) domain, an intervening region (IVR) with a double glycine region (DGR), multiple cysteines, and a C-terminal region (CTR) [26].”
Background
Binding thermodynamics and kinetics guided optimization of potent Keap1–Nrf2 peptide inhibitors
Lu, M.-C., Chen, Z.-Y., Wang, Y.-L., Jiang, Y.-L., Yuan, Z.-W., You, Q.-D., & Jiang, Z.-Y. (2015) · RSC Advances · doi:10.1039/c5ra16262a · Cited by 55
Recent progress in the development of small molecule Nrf2 activators: a patent review (2017-present)
Zhou, H.-S., Wang, Y., You, Q., & Jiang, Z. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1715365 · Cited by 53
“Human Keap1 contains five domains: N-terminal domain (NTD, 1–60); Broad complex, Tramtrack, and Bric- ́a-Brac (BTB, 61–178) domain; intervening region (IVR, 179–321); double glycine repeat (DGR, 322–608) and Kelch domain; and C-terminal region (CTR, 609–625) [20,21].”
Background
Nanotechnology-Based Drug Delivery to Improve the Therapeutic Benefits of NRF2 Modulators in Cancer Therapy
Bayındır, Z. S., Losada‐Barreiro, S., Bravo‐Díaz, C., Sova, M., Kristl, J., & Saso, L. (2021) · Antioxidants · doi:10.3390/antiox10050685 · Cited by 58
Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered
Karunatilleke, N. C., Fast, C. S., Ngo, V., Brickenden, A. M., Duennwald, M. L., Konermann, L., & Choy, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147434 · Cited by 52
“Nrf2 activity is regulated through the interactions with a suite of different proteins [4,21–27], including Kelch-like ECH-associated protein 1 (Keap1) [22,28].”
BackgroundInfluential
Exploring the links between polyphenols, Nrf2, and diabetes: A review
Ebrahimi, R., Mohammadpour, A., Medoro, A., Davinelli, S., Saso, L., & Miroliaei, M. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118020 · Cited by 61

Authors: Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M.
Affiliations: University of Missouri (US)
Corresponding author: Beamer, Lesa J
Hannink, Mark
ORCID: Lo, Shih‐Ching
Beamer, Lesa J
Hannink, Mark
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2006-08-03
Volume: 25
Issue: 15
Pages: 3605-3617
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7601243
PMC: PMC1538563
OpenAlex: W2141982524
Cited by: 604
References: 68
Citations by year: 2026: 66 · 2025: 66 · 2024: 44 · 2023: 48 · 2022: 47 · 2021: 36 · 2020: 35 · 2019: 23 · 2018: 22 · 2017: 21 · 2016: 25 · 2015: 25 · 2014: 22 · 2013: 34 · 2012: 22
FWCI: 4.63
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute (P50CA103130)
National Center for Complementary and Integrative Health (AT003899, R01AT003899)
Lawrence Berkeley National Laboratory
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: Keap1, Nrf2, Kelch domain, protein-protein interaction, beta-turn, oxidative stress response, chemoprevention, protein structure
MeSH terms: Kelch-Like ECH-Associated Protein 1, Amino Acid Sequence, Animals, Binding Sites, Cells, Cultured, Chlorocebus aethiops, Humans, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Conformation, Signal Transduction, Conserved Sequence, Protein Structure, Tertiary, Dimerization, COS Cells, Amino Acid Motifs, Intracellular Signaling Peptides and Proteins, NF-E2-Related Factor 2

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Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

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