Molecular Modeling of Licochalcone E As Protein Tyrosine Phosphatase 1b Inhibitor

Table S1. Assignment of the binding pocket in two types of PTP1B: open form and closed form. Figure S1. The binding pose of the ursolic acid in the open form (A) and the closed form of PTP1B (C). To understand the atomistic binding interaction, the ursolic acid (navy) and (R)-(+)-LicoE (sky blue) are superimposed for the open form (B) and the closed form (D). In common, the ursolic acid has more hydrophobic interactions in PTP loop. In the open form, a hydrogen bond exits in related with the backbone of A217 in PTP loop, while a hydrogen bond with the closed form is in the backbone of Asp48 in pTyr loop. The binding pocket of the open form seems like capsule consisting of pTyr loop, WPD loop, PTP loop, and Q-loop. Interestingly, Tyr263 and Lys116 look like guideline in spite of exception of the important catalytic site. Depending on the allosteric effect of WPD loop, the binding pocket of the closed form seems like the hydrophobic sandwich. The ursolic acid is between the hydrophobic cores including PTP loop, pTyr loop, and WPD loop. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.