Transfer-NMR and docking studies identify the binding of the peptide derived from activating transcription factor 4 to protein ubiquitin ligase beta-TrCP. Competition STD-NMR with β-catenin.

ATF4 plays a crucial role in the cellular response to stress. The E3 ubiquitin ligase, SCF β-TrCP protein responsible for ATF4 degradation by the proteasome, binds to ATF4 through a DpSGXXXpS phosphorylation motif, which is similar but not identical to the DpSGXXpS motif found in most other substrates of β-TrCP. NMR studies were performed on […]

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