Figure 3: Detailed characterization of the TRX–TXNIP interaction.
From: The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein
(a) The critical β18 strand (cyan) of TXNIP that interacts with TRX is shown. The cleft formed by residues in the active site of TRX is highlighted in pink. The TRX Cys32 and TXNIP Cys247 residues that form an intermolecular disulphide bond are shown as white and cyan carbon atoms, respectively. (b) Stereo image of the 2Fo-Fc electron density map showing the intermolecular disulphide bond between the TRX Cys32 (white) and TXNIP Cys247 (cyan) residues contoured at 1.5σ. (c) Detailed depiction of the interactions between TRX (white) and TXNIP (cyan). The backbone–backbone interactions between TRX Met74 and TXNIP Cys247, and TRX Ala92 and TXNIP Gly245, are displayed as dashed red lines. The salt bridge between TRX Asp60 and TXNIP Arg251 and the hydrogen bond between TRX Gly33 and TXNIP Glu202 are shown as dashed black lines. Strands β15 and β18 in TXNIP are also indicated.
