Delineating the role of c-FLIP/NEMO interaction in the CD95 network via rational design of molecular probes.

ABSTRACT:

Background

Structural homology modeling supported by bioinformatics analysis plays a key role in uncovering new molecular interactions within gene regulatory networks. Here, we have applied this powerful approach to analyze the molecular interactions orchestrating death receptor signaling networks. In particular, we focused on the molecular mechanisms of CD95-mediated NF-κB activation and the role of c-FLIP/NEMO interaction in the induction of this pathway.

Results

To this end, we have created the homology model of the c-FLIP/NEMO complex using the reported structure of the v-FLIP/NEMO complex, and rationally designed peptides targeting this complex. The designed peptides were based on the NEMO structure. Strikingly, the experimental in vitro validation demonstrated that the

SUBMITTER: Ivanisenko NV 

PROVIDER: S-EPMC6900753 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature