Extended Data Fig. 3: Eya3 binds PP2A:B55.
From: Cryo-EM structures of PP2A:B55 with p107 and Eya3 define substrate recruitment
a. Chemical Shift Index (CSI) (left) and Secondary-structure propensity (SSP) (right) data for Eya3 plotted vs. residue numbers. (SSP > 0, α helix; SSP < 0, β strand). Cα and Cβ chemical shifts were used to create the CSI and SSP plots (RefDB database)1. Preferred secondary structure indicated above SSP data. b. 2D [1H,15N] HSQC spectrum of 15N-labeled Eya327-155 (black) and Eya362-108EE (blue). Peaks do not overlap as well as expected for an IDP indicating longer range interactions in the IDR of Eya3. Insert shows Nε/HεN cross peak of W124. c. 2D [1H,15N] HSQC spectrum of 15N-labeled Eya327-155 with (pink) and without (black) PP2A:B55. Significant number of peaks are pink, corresponding to unbound Eya3 residues. Insert shows Nε/HεN cross peak of W124. d. 2D [1H,15N] HSQC spectrum of 15N-labeled Eya327-155 with (pink), without (black) PP2A:B55 and Eya362-108EE (blue), highlighting that most black peaks in (b) correspond with blue peaks from Eya362-108EE. Insert shows Nε/HεN cross peak of W124.
