Title : Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO.

Pub. Date : 2014

PMID : 24896564






3 Functional Relationships(s)
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1 We report here the first structure of the BTB domain of Keap1, which is thought to contain the key cysteine residue responsible for interaction with electrophiles, as well as structures of the covalent complex with the antagonist CDDO/bardoxolone, and of the constitutively inactive C151W BTB mutant. btb kelch like ECH associated protein 1 Homo sapiens
2 We report here the first structure of the BTB domain of Keap1, which is thought to contain the key cysteine residue responsible for interaction with electrophiles, as well as structures of the covalent complex with the antagonist CDDO/bardoxolone, and of the constitutively inactive C151W BTB mutant. btb kelch like ECH associated protein 1 Homo sapiens
3 In addition to providing the first structural confirmation of antagonist binding to Keap1 BTB, we also present biochemical evidence that adduction of Cys 151 by CDDO is capable of inhibiting the binding of Cul3 to Keap1, and discuss how this class of compound might exert Nrf2 activation through disruption of the BTB-Cul3 interface. btb kelch like ECH associated protein 1 Homo sapiens