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

Figure 8

H-bond patterns in the A-loop and the JMR.

Top: H-bonds stabilizing the small 310-helix in the A-loop of KITWT (in two different projections) and coiled structure of the A-loop observed in mutant KITD816H. Bottom: H-bonds of the JMR and the N-lobe residues stabilizing the coiled structure of the JM-Switch in KITWT and KITV560D and nearly antiparallel β-sheet in KITV560G. All residues presented as sticks, each residue is labeled in KITWT and specified by color retained for the same residue in the mutants, only the side chains participating in the H-bonds are shown. The H-bonds are shown as dotted lines.

Figure 8

doi: https://doi.org/10.1371/journal.pcbi.1003749.g008