Docking of Fatty Acids into the WIF Domain of the Human Wnt Inhibitory Factor-1

@article{Malinauskas2008DockingOF,
  title={Docking of Fatty Acids into the WIF Domain of the Human Wnt Inhibitory Factor-1},
  author={Tomas Malinauskas},
  journal={Lipids},
  year={2008},
  volume={43},
  pages={227-230}
}
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… 
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Modular mechanism of Wnt signaling inhibition by Wnt inhibitory factor 1

A modular model for the localization of WIF-1 and for signal inhibition within morphogen gradients is suggested, consistent with conserved positively charged residues on EGF IV.

Prediction of Structure of Human WNT-CRD (FZD) Complex for Computational Drug Repurposing

The dimeric cysteine-rich domain was found to fit into the evolutionarily conserved U-shaped groove of WNT protein, thus providing a strong hydrophobic moiety for the frizzled receptor and serving as the largest binding pocket for WNT-FZD interaction.

The Role of Glypicans in Wnt Inhibitory Factor-1 Activity and the Structural Basis of Wif1's Effects on Wnt and Hedgehog Signaling

Zebrafish embryos and the heterologous system provided by D. melanogaster wing are used and it is shown that the Wif1 WIF domain can increase the Hh promoting activity of Shf's EGF domains, suggesting it is capable of interacting with Hh.

Structural Insights into the Inhibition of Wnt Signaling by Cancer Antigen 5T4/Wnt-Activated Inhibitory Factor 1

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Crystal structures and WNT-binding characteristics of extracellular regions from the Drosophila ROR and RYK orthologs Nrk (neurospecific receptor tyrosine kinase) and Derailed-2 (Drl-2) provide new insight into how WNTs recruit their RTK co-receptors into signaling complexes.

WIF1 can effectively co-regulate pro-apoptotic activity through the combination with DKK1.

Wnt proteins.

The process of maturation of Wnt from its initial translation to its eventual release from a cell and interactions in the extracellular environment is described.

Secretion and extracellular space travel of Wnt proteins.

Wif-1 is expressed at cartilage-mesenchyme interfaces and impedes Wnt3a-mediated inhibition of chondrogenesis

Wif-1 is identified as a novel extracellular Wnt modulator in cartilage biology and impaired growth of mesenchymal precursor cells and neutralised Wnt3a-mediated inhibition of chondrogenesis in micromass cultures of embryonic chick limb-bud cells.

Extracellular modulators of Wnt signalling.

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