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| {{STRUCTURE_2z32| PDB=2z32 | SCENE= }} | | {{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==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_18391415}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18391415 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18391415}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| [[Category: Ubl conjugation]] | | [[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 Mon Jul 28 13:02:16 2008'' |
