2. Academic Validation
  3. Inhibition of Wnt signaling by Dishevelled PDZ peptides

Inhibition of Wnt signaling by Dishevelled PDZ peptides

  • Nat Chem Biol. 2009 Apr;5(4):217-9. doi: 10.1038/nchembio.152.
Yingnan Zhang 1,  Brent A Appleton,  Christian Wiesmann,  Ted Lau,  Mike Costa,  Rami N Hannoush,  Sachdev S Sidhu
Affiliations

Affiliation

  • 1 Department of Protein Engineering, Genentech, Inc, South San Francisco, California, USA.
PMID: 19252499 DOI: 10.1038/nchembio.152
Abstract

Dishevelled proteins are key regulators of Wnt signaling pathways that have been implicated in the progression of human cancers. We found that the binding cleft of the Dishevelled PDZ domain is more flexible than those of canonical PDZ domains and enables recognition of both C-terminal and internal Peptides. These peptide ligands inhibit Wnt/beta-catenin signaling in cells, showing that Dishevelled PDZ domains are potential targets for small-molecule Cancer therapeutics.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P10164
    PDZ Peptide
    Wnt