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PDBsum entry 2z32

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Transcription PDB id
2z32
Jmol
Contents
Protein chain
290 a.a. *
Ligands
GLN-ASN-GLU-GLU-
ASN-GLY-GLU-GLN-
GLU
SO4 ×5
Waters ×250
* Residue conservation analysis
PDB id:
2z32
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.
Resolution:
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
Date:
31-May-07     Release date:   11-Mar-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9Z2X8  (KEAP1_MOUSE) -  Kelch-like ECH-associated protein 1
Seq:
Struc:
 
Seq:
Struc:
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.
 
  ABSTRACT  
 
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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.