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 3

MD simulations of the KIT cytoplasmic domain in the inactive state.

The RMSDs (in Å) per residue were calculated from trajectories 1 (red) and 2 (green) of MD simulations of KIT^D816Y, KIT^D816N, KIT^D816H, KIT^V560G and KIT^V560G. Horizontal doted lines indicate the RMSDs mean values.

doi: https://doi.org/10.1371/journal.pcbi.1003749.g003