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Docking of Fatty Acids into the WIF Domain of the Human Wnt Inhibitory Factor‐1
Author(s) -
Malinauskas Tomas
Publication year - 2008
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-007-3144-3
Subject(s) - wnt signaling pathway , docking (animal) , inhibitory postsynaptic potential , binding site , biochemistry , binding domain , plasma protein binding , chemistry , microbiology and biotechnology , biology , computational biology , signal transduction , neuroscience , medicine , nursing
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.