Figure 1 - full size

 

Figure 1.
FIG. 1. Comparison of the structure of the catalytic domain of PTPL1 and PTP1B. A, overall ribbon structure of the PTPL1 catalytic domain (residues 2152-2485) phosphate complex (left panel). A 2 F[o] - F[c], [calc] electron density map for the phosphate molecule is drawn in red and displays well ordered density. The key features of the structure that are described under the Introduction are indicated in magenta. The N-terminal 0 helix that replaces the 7 helix on PTP1B is displayed in yellow. Shown in stick representation are Cys-2408, Asp-2378, Arg-2205, Ile-2458, and Met-2307. The electrostatic potential of the surface of PTPL1 and the location of the positively charged primary and secondary phosphotyrosine binding pockets are indicated (right panel). The blue areas (+6kT) represent highly positively charged residues, and the red areas (-6kT) represent highly negatively charged residues. B, overall ribbon structure of the PTP1B catalytic domain (residues 1-298, left panel). The electrostatic potential of the surface of PTP1B, calculated without the peptide bound to the enzyme, complexed to the phosphorylated insulin receptor peptide phosphorylated at residues equivalent to Tyr-1162 and Tyr-1163 on the insulin receptor that are located in the primary and secondary phosphotyrosine binding pockets, respectively is shown in the right panel.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 8180-8187) copyright 2005.