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. Author manuscript; available in PMC: 2020 Aug 6.
Published in final edited form as: Structure. 2019 Jun 13;27(8):1308–1315.e3. doi: 10.1016/j.str.2019.05.002

Figure 2. The E565A mutation increases localized conformational dynamics and induces allosteric changes to residues surrounding the phenylalanine within the DFG motif.

Figure 2.

(a) Comparison of generalized order parameters (S2; left axis) and 1H-1H cross-correlated relaxation rates (η; right axis) for wild-type (blue circles) and E565A (red squares). Error bars denote the error of fitted η values used to calculate S2. (b) Difference plot of S2 values (ΔS2) from panel (a) calculated by subtracting E565A values from those of wild-type FGFR2K. Note that compared to the C-lobe, several N-lobe residues display ΔS2 values significantly greater than zero. (c) ΔS2 values are mapped on corresponding methyl carbon atoms as spheres onto the inhibited structure of FGFRK (PDB ID:3KY2) represented in gray cartoon. The inset shows a zoomed-in view of the DFG latch. The range of ΔS2 is denoted by a colored boxed bar. Note the decrease in order for the methyl groups of I541 and L617 in E565E which are directly surrounding the phenylalanine from the DFG latch motif.