Modular mechanism of Wnt signaling inhibition by Wnt inhibitory factor 1.

Journal article

Wnt morphogens control embryonic development and homeostasis in adult tissues. In vertebrates the N-terminal WIF domain (WIF-1(WD)) of Wnt inhibitory factor 1 (WIF-1) binds Wnt ligands. Our crystal structure of WIF-1(WD) reveals a previously unidentified binding site for phospholipid; two acyl chains extend deep into the domain, and the head group is exposed to the surface. Biophysical and cellular assays indicate that there is a WIF-1(WD) Wnt-binding surface proximal to the lipid head group ...

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Authors: Malinauskas, T; Aricescu, A; Lu, W; Siebold, C; Jones, E

• Publication status: Published
• Journal: Nature structural and molecular biology
• Volume: 18
• Issue: 8
• Pages: 886-893
• Publication date: 2011-08-01
• DOI: 10.1038/nsmb.2081
• EISSN: 1545-9985
• ISSN: 1545-9993
• Language: English
• Keywords: Signal Transduction; Humans; Glycosaminoglycans; Models, Molecular; Protein Folding; Binding Sites; Amino Acid Motifs; HEK293 Cells; Wnt Proteins; Protein Structure, Tertiary; Lipid Metabolism; Repressor Proteins; Adaptor Proteins, Signal Transducing