Fig. 4: Structural comparison with other WIN site ligands.
From: The NTE domain of PTENα/β promotes cancer progression by interacting with WDR5 via its SSSRRSS motif
A Different WIN motif ligand peptides bind to WDR5 using the same arginine-binding pocket. Superposition of WIN motif peptides shown with a schematic representation (left), cut-away view of the arginine-binding pocket of WDR5 (middle), and zoomed view of the conserved WIN motif residues (P0 and P-1) (right). The WDR5 molecule was presented as electrostatic potential surface and the different WIN motif peptides were presented as cartoon diagram by different colors. B PTENα/β-NTE has a unique -RR- WIN site binding motif. Sequence alignment of the WIN motif peptides displayed in the complex structures. The key conserved arginine residue was highlighted in green and the conserved WIN motif residues (P0 and P-1) were represented in red character. C The unique R118 residue of the PTENα-NTE binds to the P2 pocket of WDR5. D Mutations of the PTENα-NTE-R118 residue affected binding to WDR5. ITC curves (left) and binding affinities (right) for the titration of wild-type or different R118 mutants of PTENα-NTE1–173 to WDR522–334.
