Structure of the Trehalose-6-phosphate Phosphatase from Brugia malayi Reveals Key Design Principles for Anthelmintic Drugs
Figure 7
Two binding pockets in the T6PP enzyme.
Analysis of the hypothesized binding model for trehalose 6-phosphate and enzyme kinetics suggests that inhibitors should interact with two pockets in order to maximize interactions. Trehalose 6-phosphate (A) and trehalose 6-sulfate (B) presumably bind in the phosphoryl-binding and sugar-binding pockets while glucose 6-phosphate (C) and trehalose (D) interact in only one pocket.