ArticleChemistryOpen2019
Structure-Activity Relationship of NF023 Derivatives Binding to XIAP-BIR1.
Article in ChemistryOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Reprogramming enriches for somatic cell clones with small-scale mutations in cancer-associated genes.Molecular therapy : the journal of the American Society of Gene Therapy · 2021Article
- Structure-based identification of a new IAP-targeting compound that induces cancer cell death inducing NF-κB pathway.Computational and structural biotechnology journal · 2021Article
- Structure-Activity Relationship of NF023 Derivatives Binding to XIAP-BIR1.ChemistryOpen · 2019Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inhibitors of Apoptosis Proteins (IAPs) are conserved E3-ligases that ubiquitylate substrates to prevent apoptosis and activate the NF-kB survival pathway, often deregulated in cancer. IAPs-mediated regulation of NF-kB signaling is based on the formation of protein complexes by their type-I BIR domains. The XIAP-BIR1 domain dimerizes to bind two TAB1 monomers, leading to downstream NF-kB activation. Thus, impairment of XIAP-BIR1 dimerization could represent a novel strategy to hamper cell survival in cancer. To this aim, we previously reported NF023 as a potential inhibitor of XIAP-BIR1 dimerization. Here we present a thorough analysis of NF023 binding to XIAP-BIR1 through biochemical, biophysical and structural data. The results obtained indicate that XIAP-BIR1 dimerization interface is involved in NF023 binding, and that NF023 overall symmetry and the chemical features of its central moiety are essential for an efficient interaction with the protein. Such strategy provides original hints for the development of novel BIR1-specific compounds as pro-apoptotic agents.
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