Hotspot Mutations in KIT Receptor Differentially Modulate Its Allosterically Coupled Conformational Dynamics: Impact on Activation and Drug Sensitivity

doi:10.1371/journal.pcbi.1003749

Hotspot Mutations in KIT Receptor Differentially Modulate Its Allosterically Coupled Conformational Dynamics: Impact on Activation and Drug Sensitivity

Figure 7

Variable of secondary structures in the cytoplasmic region of KIT^WT and mutants, KIT^D816H/Y/N and KIT^V560G/D.

Secondary structure assignments for the JMR (left) and the A-loop (right) were averaged over the two replica of each MD simulations (2×48 or 2×65 ns) of KIT^WT and mutants. For each residue, the proportion of each secondary structure type is given as a percentage of the total simulation time and shown with lines of different colors: 3₁₀-helices (red), antiparallel β-sheet (blue), turns (green), total structure (dashed gray).

doi: https://doi.org/10.1371/journal.pcbi.1003749.g007