2z32
From Proteopedia
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| - | + | {{STRUCTURE_2z32| PDB=2z32 | SCENE= }} | |
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'''Crystal structure of Keap1 complexed with Prothymosin alpha''' | '''Crystal structure of Keap1 complexed with Prothymosin alpha''' | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
2Z32 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z32 OCA]. | 2Z32 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z32 OCA]. | ||
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| + | ==Reference== | ||
| + | Structural analysis of the complex of Keap1 with a prothymosin alpha peptide., Padmanabhan B, Nakamura Y, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):233-8. Epub 2008 Mar 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18391415 18391415] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Acetylation]] |
| - | [[Category: | + | [[Category: B-propellor domain]] |
| - | [[Category: | + | [[Category: Cytoplasm]] |
| - | [[Category: | + | [[Category: Kelch domain]] |
| - | [[Category: | + | [[Category: Kelch repeat]] |
| - | [[Category: | + | [[Category: National project on protein structural and functional analyse]] |
| - | [[Category: | + | [[Category: Nppsfa]] |
| - | [[Category: | + | [[Category: Nrf2 regulation]] |
| - | [[Category: | + | [[Category: Nucleus]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | [[Category: | + | [[Category: Prothymosin-a interactor]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | [[Category: | + | [[Category: Ubl conjugation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:35:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:35, 30 April 2008
Crystal structure of Keap1 complexed with Prothymosin alpha
Overview
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.
About this Structure
2Z32 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the complex of Keap1 with a prothymosin alpha peptide., Padmanabhan B, Nakamura Y, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):233-8. Epub 2008 Mar 21. PMID:18391415 Page seeded by OCA on Wed Apr 30 13:35:47 2008
Categories: Mus musculus | Protein complex | Padmanabhan, B. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | Acetylation | B-propellor domain | Cytoplasm | Kelch domain | Kelch repeat | National project on protein structural and functional analyse | Nppsfa | Nrf2 regulation | Nucleus | Phosphorylation | Prothymosin-a interactor | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Transcription | Transcription regulation | Ubl conjugation
