title: Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1.
abstract: 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.
authors.affiliation: Faculty of Chemistry, Vilnius University, Vilnius, Lithuania. tomas.malinauskas@gmail.com
authors.forename: Tomas
authors.initials: T
authors.lastname: Malinauskas
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D054878:Lipoylation; D019308:Palmitic Acid / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D013816:Thermodynamics; D051153:Wnt Proteins / Q000378:metabolism*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D012097:Repressor Proteins; C485569:WIF1 protein, human; D051153:Wnt Proteins; D019308:Palmitic Acid