1qz7
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(New page: 200px<br /> <applet load="1qz7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qz7, resolution 2.20Å" /> '''Beta-catenin bindin...)
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Revision as of 16:51, 12 November 2007
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Beta-catenin binding domain of Axin in complex with beta-catenin
Contents |
Overview
The "beta-catenin destruction complex" is central to canonical, Wnt/beta-catenin signaling. The scaffolding protein Axin and the tumor, suppressor adenomatous polyposis coli protein (APC) are critical, components of this complex, required for rapid beta-catenin turnover. We, determined the crystal structure of a complex between beta-catenin and the, beta-catenin-binding domain of Axin (Axin-CBD). The Axin-CBD forms a helix, that occupies the groove formed by the third and fourth armadillo repeats, of beta-catenin and thus precludes the simultaneous binding of other, beta-catenin partners in this region. Our biochemical studies demonstrate, that, when phosphorylated, the 20-amino acid repeat region of APC competes, with Axin for binding to beta-catenin. We propose that a key function of, APC in the beta-catenin destruction complex is to remove phosphorylated, beta-catenin product from the active site.
Disease
Known diseases associated with this structure: Colorectal cancer OMIM:[116806], Hepatoblastoma OMIM:[116806], Hepatocellular carcinoma OMIM:[116806], Ovarian carcinoma, endometrioid type OMIM:[116806], Pilomatricoma OMIM:[116806]
About this Structure
1QZ7 is a Protein complex structure of sequences from Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex., Xing Y, Clements WK, Kimelman D, Xu W, Genes Dev. 2003 Nov 15;17(22):2753-64. Epub 2003 Nov 4. PMID:14600025
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