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. 2019 Oct 31;58(50):17986–17993. doi: 10.1002/anie.201908655

Figure 3.

Figure 3

MD simulations of wt7D12 and its photocaged mutants show that wt7D12 and 7D12pcY109 form more stable complexes with EGFR domain III as compared to 7D12pcY32 and 7D12pcY113. A) Simulation snapshots taken at intervals of 30 ns during 300 ns simulations for each system, (EGFR: grey for all, wt7D12: black, 7D12pcY32: red, 7D12pcY109: green, 7D12pcY113: blue) highlight the extent of motion of 7D12. B) Left: RMSDs from starting structure for protein Cα atoms during simulations show large deviations for 7D12pcY32 and 7D12pcY113. Right: The R30–D355 salt‐bridge (residues shown in (A) wt7D12 snapshot, in yellow), monitored as the distance between the R30 guanidine C and the D355 carboxyl C, breaks frequently in the 7D12pcY32 and 7D12pcY113 systems. These observations suggest that the presence of pcY at positions 32 and 113 destabilizes the 7D12–EGFR domain III complex.