Characterization of a Wnt-binding site of the WIF-domain of Wnt inhibitory factor-1

L. Bányai, Krisztina Kerekes, L. Patthy

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A Wnt-binding site of the WIF-domain of Wnt inhibitory factor-1 was localized by structure-guided arginine-scanning mutagenesis in combination with surface plasmon resonance assays. Our observation that substitution of some residues of WIF resulted in an increased affinity for Wnt5a, but decreased affinity for Wnt3a, suggests that these residues may define the specificity spectrum of WIF for Wnts. These results hold promise for a more specific targeting of Wnt family members with WIF variants in various forms of cancer. Structured summary of protein interactions: WIF binds to Wnt7a by surface plasmon resonance (View Interaction) WIF binds to Wnt4 by surface plasmon resonance (View Interaction) WIF and Wnt3a physically interact by competition binding (View Interaction 1, 2, 3, 4,5, 6) WIF binds to Wnt9b by surface plasmon resonance (View Interaction) WIF binds to Wnt5a by surface plasmon resonance (View Interaction) WIF binds to Wnt11 by surface plasmon resonance (View Interaction) WIF binds to Wnt3a by surface plasmon resonance (View Interaction) Wnt-5a and WIF physically interact by competition binding (View Interaction 1,2, 3, 4, 5, 6).

Original languageEnglish
Pages (from-to)3122-3126
Number of pages5
JournalFEBS Letters
Volume586
Issue number19
DOIs
Publication statusPublished - Sep 21 2012

Fingerprint

Wnt Proteins
Surface Plasmon Resonance
Surface plasmon resonance
Binding Sites
Mutagenesis
Arginine
Assays
Substitution reactions
Scanning

Keywords

  • Cancer
  • Protein-protein interaction
  • WIF-domain
  • Wnt
  • Wnt inhibitory factor- 1

ASJC Scopus subject areas

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

Cite this

Characterization of a Wnt-binding site of the WIF-domain of Wnt inhibitory factor-1. / Bányai, L.; Kerekes, Krisztina; Patthy, L.

In: FEBS Letters, Vol. 586, No. 19, 21.09.2012, p. 3122-3126.

Research output: Contribution to journalArticle

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