2Z32: Crystal Structure Of Keap1 Complexed With Prothymosin Alpha

Citation:
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2008) 64 p.233-238
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.
PDB ID: 2Z32Download
MMDB ID: 62952
PDB Deposition Date: 2007/5/31
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2Z32: dimeric; determined by author and by software (PISA)
Molecular Components in 2Z32
Label Count Molecule
Proteins (2 molecules)
1
Kelch-like Ech-associated Protein 1(Gene symbol: Keap1)
Molecule annotation
1
Prothymosin Alpha(Gene symbol: Ptma)
Molecule annotation
Chemicals (5 molecules)
1
5
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.