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… Expand
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Modular mechanism of Wnt signaling inhibition by Wnt inhibitory factor 1
TLDR
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. Expand
Prediction of Structure of Human WNT-CRD (FZD) Complex for Computational Drug Repurposing
TLDR
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. Expand
The Role of Glypicans in Wnt Inhibitory Factor-1 Activity and the Structural Basis of Wif1's Effects on Wnt and Hedgehog Signaling
TLDR
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. Expand
Structural Insights into the Inhibition of Wnt Signaling by Cancer Antigen 5T4/Wnt-Activated Inhibitory Factor 1
TLDR
Crystal structures for the extracellular domain of 5T4/WAIF1 reveal a highly glycosylated, rigid core, comprising eight leucine-rich repeats (LRRs), which serves as a platform to present evolutionarily conserved surface residues in the N-terminal LRR1. Expand
ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes.
TLDR
Crystal structures and WNT-binding characteristics of extracellular regions from the Drosophila ROR and RYK orthologs Nrk and Derailed-2 are described, providing further insight into how WNTs may recruit RTK co-receptors into signaling complexes. Expand
ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes
TLDR
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. Expand
WIF1 can effectively co-regulate pro-apoptotic activity through the combination with DKK1.
TLDR
The results indicate for the first time that the tumor suppressor WIF1 is involved in angiogenesis and supplies a possible molecular target for the treatment of distinct malignant cancers, as well as several other associated diseases. Expand
Wnt proteins.
TLDR
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. Expand
Secretion and extracellular space travel of Wnt proteins.
TLDR
Recent discoveries on factors and processes implicated in Wnt secretion, a highly complex, regulated secretory process that guides Wnt proteins through the exocytic pathway are reviewed. Expand
Wif-1 is expressed at cartilage-mesenchyme interfaces and impedes Wnt3a-mediated inhibition of chondrogenesis
TLDR
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. Expand
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