Figure 6
From: Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State
Binding configuration for CypD and Prx3 or Trx2.
Panels (A–C) show the best predicted binding of CypD and Prx3. Panel (A) is the global view of the best binding. Panel (B) shows the details of the pocket and one can notice the protrusion of Phe-107 of Prx3 in the hydrophobic pocket of CypD and also are highlighted the residues of CypD that interact with it. Cys-157 of CypD is shown in green while Cys-109 of Prx3 is shown in orange. Panel (C) highlights the possible salt bridges formed by the two molecules, in particular those formed by Asp-104 and Asp-136 of Prx3 with Lys-167 of CypD. Panels (D–F) show the binding of CypD to Trx2. Panel (D) is the global view of the best predicted binding. As one can see in Panel (E), the interaction of Trp-89 with the hydrophobic pocket is more superficial compared to that of Prx3. The position of Cys-157 of CypD is shown in green, while Cys-90 and Cys-93 of Trx2 are shown in purple. In Panel (F), the possible salt bridges that could stabilize the interaction between the two proteins are reported: Arg-97 of CypD with Asp-120 of Trx2 and Lys-190 of CypD with Asp-66 or Asp-123 of Trx2. The amino acids residues are labelled according to full-length proteins sequence.
