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

Pub. Date : 2014

PMID : 24896564






1 Functional Relationships(s)
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1 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 cullin 3 Homo sapiens