Fig. 6
From: Self-regulation of functional pathways by motifs inside the disordered tails of beta-catenin
Disordered tails regulate the function of beta-Catenin in two pathways. (A) Key players in the cadherin junction formation pathway and the Wnt signaling pathway. Proteins in red color are intrinsically disordered, while proteins in blue color are basically structured. Beta-Catenin was shown in dark blue to be differentiated from other proteins. Cadherin was shown in apricot due to its large amount of intrinsically disordered residues. (B) Regulatory roles of disordered tails on the functions of beta-Catenin in both cadherin junction formation and Wnt signaling pathways. ARM is the armadillo domain of beta-Catenin. N-ter and C-ter stand for the N-terminal and C-terminal tails of beta-Catenin. (a) – (e) represent five different functional stages of beta-Catenin. “P” indicates phosphorylation. “FG” stands for phenylalanine-glycine(FG)-repeat containing proteins in the nuclear pore complex. “NTM” refers to nuclear translocation motif. The destruction complex is composed of CKI-alpha, GSK-3beta, Axin, and APC. (C) Conserved sequential patterns among mouse cadherin (UniPortKB Entry: P09803, AA813-834), human cadherin (UniPortKB Entry: P12830, AA811-832), mouse beta-Catenin (UniProtKB Entry: Q02248, AA751-781), and human beta-Catenin (UniPortKB Entry: P35222, AA751-781). (D) Pocket formed by AA400-663 (PDB id: 1JDN). Blue: positive charged residues; Red: negative charge residues; Gray: hydrophobic residues; Light yellow: other residues. (E) Change of the direction of the line formed between the oxygen atom on the side chain of Tyr654 and the Cα atom of Tyr432 in two PDB structures (Blue: PDB 2Z6H; Apricot: PDB 1QZ7). The angle associated with the change of the direction implies the structural variation of the binding pocket. The RMSD calculated from these two structures for the segment from AA576 to AA685 is 0.75 angstroms