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Sci. Signal., 10 July 2012
Vol. 5, Issue 232, p. ec187
[DOI: 10.1126/scisignal.2003373]


Structural Biology Dissecting Wnt/Fz Interaction

Valda K. Vinson

Science, AAAS, Washington, DC 20005, USA.

Wnt proteins activate the transmembrane receptor Frizzled (Fz) to initiate pathways central to vertebrate and invertebrate development. Wnts are palmitoylated, which has complicated structural and functional characterization. Janda et al. (see the Perspective by Bienz and He) achieved coexpression and purification of Xenopus Wnt8 (XWnt8) with mouse Fz8 cysteine rich domain (CRD) and determined a crystal structure of the complex. Wnt binds to the Fz8 CRD at two distinct sites with the lipid group playing a key role in the first interface. Both interfaces involve conserved amino acids, which may explain the known pleiotropy of the Wnt/Fz interaction.

C. Y. Janda, D. Waghray, A. M. Levin, C. Thomas, K. C. Garcia, Structural basis of Wnt recognition by Frizzled. Science 337, 59–64 (2012). [Abstract] [Full Text]

M. Bienz, X. He, A lipid linchpin for Wnt-Fz docking. Science 337, 44–45 (2012). [Abstract] [Full Text]

Citation: V. K. Vinson, Dissecting Wnt/Fz Interaction. Sci. Signal. 5, ec187 (2012).

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