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. 2014 Apr 8;2014:653487. doi: 10.1155/2014/653487

Figure 8.

Figure 8

Structural modeling and dynamics profile of L858R EGFR mutant. (a) The dynamics profile of the inactive wild-type EGFR (pdb id 1XKK). (b) The dynamics profile of the active wild-type EGFR (pdb id 2J6M) crystal structure of the wild-type EGFR. (c) The structural model and dynamics profile of the L858R mutant. The L858, L858R, and L861 residues are shown in sticks and colored according to their mobility profile. The hydrophobic regulatory spine residues (M766-L777-H835-F856-D896) are shown in spheres. Structural distribution of the protein kinase mobility is averaged over the two lowest frequency modes obtained from all-atom MD simulations. A surface-based protein representation is employed, colored (blue-to-red) according to the protein residue motilities (from more rigid-blue regions to more flexible-red regions).