Structural Basis of β-Catenin Recognition by Tax-interacting Protein-1

Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins

“…8D). An additional commonality to our result with claudin-2 showed that mutation of the tryptophan (in the case to an alanine) reduces the binding affinity by 100-fold (33). A similar change in the PDZ ␤2-␤3 loop conformation between the unbound and its ligand-bound state was observed with the PDZ of SHANK1 (34).…”

“…Recently it was shown that the Tax-interacting protein-1 (TIP1) undergoes a conformational change in its ␤2-␤3 loop upon binding of ligand ␤-catenin (Fig. 8C) (33). In the case of ␤-catenin binding to TIP1, it is its tryptophan residue at P Ϫ5 that displaces the ␤2-␤3 loop of the TIP1 PDZ domain.…”

Molecular Mechanism of Inward Rectifier Potassium Channel 2.3 Regulation by Tax-Interacting Protein-1

“…29 Full-length TIP-1 contains only one PDZ domain; it has the canonical PDZ domain fold composed of six β-strands (termed βA-F) and two α-helices (αA and αB), of which the six β-strands form a partially open barrel with each of the open ends capped with an α-helix ( Fig. 1a and c).…”

“…27 TIP-1 is devoid of protein-protein interaction modules except for a single PDZ domain and acts as a negative regulator of the Wnt/β-catenin signaling pathway because of its very high β-catenin binding affinity. 28,29 TIP-1 has also been shown to uncouple Kir2.3 channels from basolateral membranes, causing them to accumulate in recycling vesicles. 19 The internalization of Kir2.3 channels, on the other hand, has been shown to be clathrin mediated and to involve dynamin through a novel signal located within Kir2.3's C-terminal region, which is upstream of its PDZ-binding motif.…”

The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6

“…Similar observations have been made in other studies. 34,[52][53][54] We previously showed that the mutation of the C-terminal leucine residue into a valine resulted in a significant gain in affinity, 32 which proves beneficial for the detection of intermolecular nuclear Overhauser enhancements (NOEs). Our present studies were therefore performed using a chimeric peptide composed of the 11 C-terminal residues of HPV16 E6 (sequence RSSRTRRETQV, hereafter named 16E6 ct L 0 /V †).…”