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. 2019 Jul 24;294(38):13964–13972. doi: 10.1074/jbc.RA119.009131

Figure 5.

Figure 5.

Interaction between KRASV14I and SOS1. A, the binding interface of KRASV14I for SOS1 based on PDB 1NVU. Interacting residues on KRASV14I are highlighted in red. B, SOS1:KRAS binding affinity as measured by microscale thermophoresis. KRASV14I shows enhanced affinity toward SOS1 relative to KRASWT. All measurements were performed in triplicate: Kd for WT is 8.3 ± 0.6 (μm) and V14I is 0.22 ± 0.1 (μm). The SOS1 construct includes the REM and catalytic domains.