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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.
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