1QZ7

Beta-catenin binding domain of Axin in complex with beta-catenin

Summary for 1QZ7

• Entry DOI: 10.2210/pdb1qz7/pdb
• Descriptor: Beta-catenin, Axin (3 entities in total)
• Functional Keywords: beta-catenin, axin, protein-protein complex, cell adhesion
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P35222; Cytoplasm (By similarity): Q9YGY0
• Total number of polymer chains: 2
• Total formula weight: 65968.03

Authors

Xing, Y.,Clements, W.K.,Kimelman, D.,Xu, W. (deposition date: 2003-09-15, release date: 2003-11-18, Last modification date: 2023-08-23)

Primary citation

Xing, Y.,Clements, W.K.,Kimelman, D.,Xu, W.
Crystal structure of a beta-catenin/Axin complex suggests a mechanism for the {beta}-catenin destruction complex
GENES DEV., 17:2753-2764, 2003

PubMed Abstract: 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.

PubMed: 14600025
DOI: 10.1101/gad.1142603

Experimental method

X-RAY DIFFRACTION (2.2 Å)