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

FEBS Letters
Krisztina KerekesL Patthy

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.

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Citations

Sep 1, 2016·Annual Review of Cell and Developmental Biology·Elena SeiradakeRüdiger Klein
Mar 1, 2017·British Journal of Pharmacology·Else Driehuis, Hans Clevers
Feb 18, 2017·Current Opinion in Hematology·Lina Badimon, Maria Borrell-Pages
Oct 21, 2018·Journal of Cellular Physiology·Vahid HosseiniMasoud Darabi
Aug 31, 2021·Signal Transduction and Targeted Therapy·Fanyuan YuLing Ye

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