NMR structure of the WIF domain of the human Wnt-inhibitory factor-1

Edvards Liepinsh, László Bányai, László Patthy, Gottfried Otting

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The human Wnt-binding protein Wnt-inhibitory factor-1 (WIF-1) comprises an N-terminal WIF module followed by five EGF-like repeats. Here we report the three-dimensional structure of the WIF domain of WIF-1 determined by NMR spectroscopy. The fold consists of an eight-stranded β-sandwich reminiscent of the immunoglobulin fold. Residual detergent (Brij-35) used in the refolding protocol was found to bind tightly to the WIF domain. The binding site was identified by intermolecular nuclear Overhauser effects observed between the WIF domain and the alkyl chain of the detergent. The results point to a possible role of WIF domains as a recognition motif of Wnt and Drosophila Hedgehog proteins that are activated by palmitoylation.

Original languageEnglish
Pages (from-to)942-950
Number of pages9
JournalJournal of molecular biology
Volume357
Issue number3
DOIs
Publication statusPublished - Mar 31 2006

Keywords

  • NMR spectroscopy
  • Palmitoylation
  • Three-dimensional structure
  • WIF domain
  • Wnt

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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