Just published in Structure. To enable NMR-based drug discovery on cFLIP, an important pro-survival factor in the extrinsic apoptosis pathway, we engineered a soluble DED1 domain, “borrowing” a sequence from the soluble DED of FADD.
We solved the solution structure of the engineered DED1 domain of cFLIP by NMR and CS-ROSETTA and used NMR-based methods to map the binding interface with DISC partners.
Stay tuned for our ongoing studies on inhibitors discovery through NMR-based fragment screening: we are interested in testing the effect of our inhibitors on DISC assembly and caspase-8 activation.
An engineered construct of cFLIP provides insight into DED1 structure and interactions
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