PDBsum entry 2z32

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Transcription PDB id
Protein chain
290 a.a. *
SO4 ×5
Waters ×250
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of keap1 complexed with prothymosin alpha
Structure: Kelch-like ech-associated protein 1. Chain: a. Fragment: keap1-dc, unp residues 309-607. Synonym: cytosolic inhibitor of nrf2, inrf2, keap1. Engineered: yes. Prothymosin alpha. Chain: b. Fragment: prothymosin-a peptide, unp residues 39-54. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: keap1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic peptide. This sequence occurs naturally in mouse.
2.00Å     R-factor:   0.169     R-free:   0.223
Authors: B.Padmanabhan,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: B.Padmanabhan et al. (2008). Structural analysis of the complex of Keap1 with a prothymosin alpha peptide. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 233-238. PubMed id: 18391415
31-May-07     Release date:   11-Mar-08    
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Protein chain
Pfam   ArchSchema ?
Q9Z2X8  (KEAP1_MOUSE) -  Kelch-like ECH-associated protein 1
624 a.a.
290 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


Acta Crystallogr Sect F Struct Biol Cryst Commun 64:233-238 (2008)
PubMed id: 18391415  
Structural analysis of the complex of Keap1 with a prothymosin alpha peptide.
B.Padmanabhan, Y.Nakamura, S.Yokoyama.
The Nrf2 transcription factor, which plays important roles in oxidative and xenobiotic stress, is negatively regulated by the cytoplasmic repressor Keap1. The beta-propeller/Kelch domain of Keap1, which is formed by the double-glycine repeat and C-terminal region domains (Keap1-DC), interacts directly with the Neh2 domain of Nrf2. The nuclear oncoprotein prothymosin alpha (ProTalpha) also interacts directly with Keap1 and may play a role in the dissociation of the Keap1-Nrf2 complex. The structure of Keap1-DC complexed with a ProTalpha peptide (amino acids 39-54) has been determined at 1.9 A resolution. The Keap1-bound ProTalpha peptide possesses a hairpin conformation and binds to the Keap1 protein at the bottom region of the beta-propeller domain. Complex formation occurs as a consequence of their complementary electrostatic interactions. A comparison of the present structure with recently reported Keap1-DC complex structures revealed that the DLG and ETGE motifs of the Neh2 domain of Nrf2 and the ProTalpha peptide bind to Keap1 in a similar manner but with different binding potencies.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19726686 C.H.Gray, L.C.McGarry, H.J.Spence, A.Riboldi-Tunnicliffe, and B.W.Ozanne (2009).
Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site for Lasp-1 that is necessary for pseudopodial extension.
  J Biol Chem, 284, 30498-30507.
PDB code: 2woz
18717629 M.J.Calkins, D.A.Johnson, J.A.Townsend, M.R.Vargas, J.A.Dowell, T.P.Williamson, A.D.Kraft, J.M.Lee, J.Li, and J.A.Johnson (2009).
The Nrf2/ARE pathway as a potential therapeutic target in neurodegenerative disease.
  Antioxid Redox Signal, 11, 497-508.  
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