fig6
![Emerging consensus on the mechanism of polyspecific substrate recognition by the multidrug transporter P-glycoprotein](https://image.oaes.cc/98c90cd1-0835-405c-90d1-b44d756d6134/3135.fig.6.jpg)
Figure 6. Plasticity of P-gp’s drug-binding surface (A) The binding environment of the cyclic inhibitor QZ-Val in the mP-gp structure with DCOM of 45 Å (PDB:4M2T). The structure is rendered as a semi-transparent electrostatic surface with bound QZ-Val shown as stick models. The membrane bilayer is indicated by the two parallel horizontal lines. The inset is a magnified inhibitor binding environment viewed from the cytosolic side of P-gp toward the extracellular side. The bound whole QZ-Val is labeled as QZ-Val-1 and the half molecule is labeled as QZ-Val-2. (B) A different binding environment of the cyclic inhibitor QZ-Val in the mP-gp structure with DCOM of 60 Å (PDB:4Q9J). There are three modeled QZ-Val molecules labeled as QZ-Val-1’, QZ-Val-2’ and QZ-Val-3’