2008/02/06 by Tomas Malinauskas · 2 citations
Biochemistry, Genetics and Molecular Biology · #Wnt/β-catenin signaling in development and cancer #Cancer-related gene regulation #Polyamine Metabolism and Applications
paper · doi:10.1007/s11745-007-3144-3
openalex publication_date 2008/02/06 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Palmitoylated Wnt proteins comprise a conserved family of secreted signaling molecules associated with variety of human cancers. WIF domain of the human WIF (Wnt inhibitory factor)-1 is sufficient for Wnt binding and signaling inhibition. Detailed interactions between Wnt and WIF-1 are not known. Computational docking was employed to identify a possible fatty acid binding site in the WIF domain. A putative binding site was identified inside the domain. WIF domain exhibited the highest affinity for C16:0-C18:0 (-22 kJ/mol free energy of binding) fatty acids. The results suggest a role of the WIF domain as a palmitoyl binding domain required for WIF-1 binding to palmitoylated Wnt and signaling inhibition.