Wnts grasp the WIF domain of Wnt Inhibitory Factor 1 at two distinct binding sites

Krisztina Kerekes, László Bányai, László Patthy

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Wnts have a structure resembling a hand with "thumb" and "index" fingers that grasp the cysteine rich domains of Frizzled receptors at two distinct binding sites. In the present work we show that the WIF domain of Wnt Inhibitory Factor 1 is also bound by Wnts at two sites. Using C-terminal domains of Wnt5a and Wnt7a and arginine-scanning mutagenesis of the WIF domain we demonstrate that, whereas the N-terminal, lipid-modified "thumb" of Wnts interacts with the alkyl-binding site of the WIF domain, the C-terminal domain of Wnts (Wnt-CTD) binds to a surface on the opposite side of the WIF domain.

Original languageEnglish
Article number37341
Pages (from-to)3044-3051
Number of pages8
JournalFEBS letters
Volume589
Issue number20
DOIs
Publication statusPublished - Oct 7 2015

Keywords

  • Arginine-scanning mutagenesis
  • Cancer therapy
  • Homology modeling
  • Protein-protein interaction
  • Ryk receptor tyrosine kinase
  • WIF domain
  • Wnt
  • Wnt Inhibitory Factor 1

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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