1qz7: Difference between revisions
New page: left|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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[[Image:1qz7.gif|left|200px]]<br /> | [[Image:1qz7.gif|left|200px]]<br /><applet load="1qz7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1qz7, resolution 2.20Å" /> | caption="1qz7, resolution 2.20Å" /> | ||
'''Beta-catenin binding domain of Axin in complex with beta-catenin'''<br /> | '''Beta-catenin binding domain of Axin in complex with beta-catenin'''<br /> | ||
==Overview== | ==Overview== | ||
The "beta-catenin destruction complex" is central to canonical | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1QZ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http:// | 1QZ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZ7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Clements, W | [[Category: Clements, W K.]] | ||
[[Category: Kimelman, D.]] | [[Category: Kimelman, D.]] | ||
[[Category: Xing, Y.]] | [[Category: Xing, Y.]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:19 2008'' | ||
Revision as of 12:45, 21 February 2008
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Beta-catenin binding domain of Axin in complex with beta-catenin
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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