Literature DB >> 18256869

Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1.

Tomas Malinauskas1.   

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.

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Year:  2008        PMID： 18256869     DOI： 10.1007/s11745-007-3144-3

Source DB:  PubMed          Journal:  Lipids        ISSN： 0024-4201            Impact factor:   1.880


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