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

@article{Malinauskas2007DockingOF,
  title={Docking of Fatty Acids into the WIF Domain of the Human Wnt Inhibitory Factor-1},
  author={Tomas Malinauskas},
  journal={Lipids},
  year={2007},
  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.

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

ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes

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.

The Drosophila WIF1 homolog Shifted maintains glypican-independent Hedgehog signaling and interacts with the Hedgehog co-receptors Ihog and Boi

It is shown here that Shf maintains short-range Hh signaling in the wing via a mechanism that does not require the presence of or binding to the Drosophila glypicans Dally and Dally-like protein.

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