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TitleInteraction Energetics and Druggability of the Protein-Protein Interaction between Kelch-like ECH-Associated Protein 1 (KEAP1) and Nuclear Factor Erythroid 2 Like 2 (Nrf2).
Journal, issue, pagesBiochemistry, Vol. 59, Page 563-581, Year 2020
Publish dateJul 12, 2017 (structure data deposition date)
AuthorsZhong, M. / Lynch, A. / Muellers, S.N. / Jehle, S. / Luo, L. / Hall, D.R. / Iwase, R. / Carolan, J.P. / Egbert, M. / Wakefield, A. ...Zhong, M. / Lynch, A. / Muellers, S.N. / Jehle, S. / Luo, L. / Hall, D.R. / Iwase, R. / Carolan, J.P. / Egbert, M. / Wakefield, A. / Streu, K. / Harvey, C.M. / Ortet, P.C. / Kozakov, D. / Vajda, S. / Allen, K.N. / Whitty, A.
External linksBiochemistry / PubMed:31851823
MethodsX-ray diffraction
Resolution1.91 - 2.5 Å
Structure data

PDB-5wfl:
Kelch domain of human Keap1 in open unliganded conformation
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-5wfv:
Kelch domain of human Keap1 bound to Nrf2 ETGE peptide
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

PDB-5wg1:
Kelch domain of human Keap1 bound to mutant Nrf2 EAGE peptide
Method: X-RAY DIFFRACTION / Resolution: 2.021 Å

PDB-5whl:
Kelch domain of human Keap1 bound to inhibitory small molecule fragment: hydroxyphenyl propionic acid
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5who:
Kelch domain of human Keap1 bound to small molecule inhibitor fragment: 4-oxo-4H-1-benzopyran-2-carboxylic acid
Method: X-RAY DIFFRACTION / Resolution: 2.23 Å

PDB-5wiy:
Kelch domain of human Keap1 bound to small molecule inhibitor fragment: 4-amino-1,7-dihydro-6H-pyrazolo[3,4-d]pyrimidine-6-thione
Method: X-RAY DIFFRACTION / Resolution: 2.23 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-HPP:
HYDROXYPHENYL PROPIONIC ACID

ChemComp-AO7:
4-oxo-4H-1-benzopyran-2-carboxylic acid

ChemComp-1XM:
4-amino-1,7-dihydro-6H-pyrazolo[3,4-d]pyrimidine-6-thione

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / Scaffold / Unliganded / Peptide-bound / TRANSCRIPTION/INHIBITOR / Inhibitor / Fragment / TRANSCRIPTION-INHIBITOR complex

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