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Beta-catenin 781 amino acid residues

Armadillo repeat: A core region composed of 12 copies of a 42 amino acid sequence motif (residues 138-664) (Huber).


N-terminal:The primary structure of b-catenin consist of an NH2-terminal portion of approximately 130 amino acids(126-138 shown).The N-terminal connects b-catenin/E-cadheren complex to a a-catenin - key regulator of the actin cytoskeleton.
Four serine/threonine residues (S33, S37, T41 and S45) at this region are well conserved and conform to the consensus GSK-3
phosphorylation site. The phosho-S/T residues are critical of b-catenin recognitin by the F box protein B-Trcp ubiquitin ligase.

  The first amino acid residues of the b-catenin C-terminal domain is referred as Helix C (residues 667-683). The Helix C (Leu673, Leu677, Leu681) packs against otherwise exposed hydrophobic residues from the last armadillo repeat, capping the c-terminal of the b-catenin main core. Lys671 and Arg684 attach to armadillo repeats through hydrogen bonds.
Helix C is important for the transactivation domain of Wnt-responsive genes, but not the turnover ob b-catenin through APC and cell adhesion through cadherens.


Crystal structure of a full-length beta-catenin
Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W
Cell Structure 2008 (PubMed)

2Z6G (PDB)

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