Molecular Dynamics Simulations of A27S and K120A Mutated PTP1B Reveals Selective Binding of the Bidentate Inhibitor

Figure 5

Residue interactions and conformational changes at the second pTyr binding site. Residue interaction networks for the (a) WT, (b) A27S, and (c) K120A systems showing the interactions at the second pTyr binding site. The blue line represents the H-bond, the gray line represents the van der Waals interaction, the pink solid line represents the salt bridge, and the magenta dotted line represents the generic contact with their closest atom. (d) Average structures of the WT, A27S, and K120A systems superimposed at the second pTyr binding site, shown in green, yellow, and blue, respectively. The distances between (e) the Nη2 atom of Arg254 and the O4/Cβ atom of the Ser27/Ala27, (f) the Cζ atom of Arg24 and the Cζ atom of Arg254, (g) the Nη1 atom of Arg254 and the O7 atom of the ligand, and (h) the Nη2 atom of Arg24 and the O7 atom of the ligand.

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