Fig. 2: Crystal structure of WDR522–334 in complex with PTENα-NTE1–173.
From: The NTE domain of PTENα/β promotes cancer progression by interacting with WDR5 via its SSSRRSS motif
A Overall structure of WDR5 in complex with PTENα-NTE. The structure was shown in cartoon with WDR5 colored in slate and PTENα-NTE colored in yellow. B Fo-Fc omit map of PTENα-NTE contoured at 1σ level. C Intramolecular hydrogen bonds stabilize the WDR5-PTENα-NTE interaction. D Detailed interaction between PTENα-NTE and WDR5. Amino acid residues of WDR5 involved in the PTENα-NTE interaction were shown as sticks and the detailed interactions were shown by enlarged views. Key hydrogen bonds were depicted as red dash lines and key water molecules were indicated as red sphere. E, F Electrostatic potential surface view of WDR5 in complex with PTENα-NTE. The PTENα-NTE was shown as cartoon (E) and sticks (F), respectively. Five WIN motif binding pockets (P1–P5) in WDR5 were labeled with green (F).
