Figure 5
From: On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEF
The impact of mutations in the linker region on its interaction with the DH domain and with RhoA. (A) comparison of 600 MHz 1H-15N TROSY-HSQC spectra of PRG672–1081 (black), the two mutants: PRG3R (red) and PRG4R (blue) and DH-PH (green); (B) plot of chemical shift differences (ΔσHN) within DH domain induced by the wild-type linker (black), PRG3R (red) and PRG4R mutants (blue); (C) comparison of 600 MHz 1H-15N TROSY-HSQC spectra of 2H,15N-RhoA in complex with wild-type PRG672–1081 (red) and PRG4R (black); several amides with the largest chemical shift perturbations are circled, peaks labeled with asterisks could not be identified in the spectrum of PRG4R; (D) surface charge distribution calculated for the crystal structure of DH-PH/RhoA complex; the putative position of the linker is shown in yellow; side chains of acidic residues within the linker are shown in space filling representation; RhoA is delineated by a green boundary for clarity.