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. 2017 May 1;31(9):904–915. doi: 10.1101/gad.300053.117

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© 2017 Ji et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 4. — Crystal structure of AXIN1 in complex with SIAH1. (A) ITC analysis of the interaction between SIAH1-SBD and AXIN1 peptide. (B) The overall structure of the AXIN1/SIAH1 complex. The sequence of the observable part of AXIN1 in the structure is ³⁷⁷VPKEVRVEPQK³⁸⁷. (C) The surface electrostatic view between AXIN1 (377–387) and SIAH1 β0, β1, and β2 sheets is shown. (D) Major interactions between AXIN1 (377–387) and SIAH1. (E) GST pull-down analysis of the interaction between SIAH1 mutants and GST-tagged AXIN1. (F) The Siah1a 3A mutant (L176A/D177A/W178A) blocks the interaction with Axin1 in the coimmunoprecipitation assay. (G) Overexpression of Siah1a, but not the 3A mutant, enhances Wnt3a-induced STF reporter. Error bars denote the SD between four replicates. (H) Overexpression of Siah1a, but not the 3A mutant, promotes degradation of Axin1.