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. 2005 Dec 7;78(2):279–290. doi: 10.1086/499925

Figure 4.

Figure 4

MD simulations. A, Comparison between the crystallographic structure of SHP-2 (gray) and the conformation attained at the end of simulations by the E76K (blue) and A72V (red) SHP-2 mutants. The N-SH2 domain and the signature motif of the PTP domain (residues 457–467) are depicted with a ribbon representation. B, RMSD of the N-SH2 loop (residues 58-62) from its starting position. Translational and rotational motions of the protein were removed by fitting the positions of the PTP signature motif atoms to their coordinates in the initial structure. A72V (red), A72S (green), E76K (blue), E76D (cyan), and wild-type (light and dark gray) SHP-2 proteins. C, Electrostatic energy between residue 76 and the PTP domain (upper panel) and solvent-accessible surface area of the PTP signature motif (lower panel) during simulations with the E76K (blue) and wild-type (black) SHP-2 proteins. D, Time behavior during simulations of the H-bonds between residues N58-Q506, G60-Q510, and A72-Q506, contributing to stabilize the interaction between the N-SH2 loop and the PTP active site, in the A72V (red) and wild-type (black) SHP-2 proteins.