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

Edvards Liepinsh, László Bányai, László Patthy, Gottfried Otting*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    40 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 - 31 Mar 2006

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