Figure 6: The interaction between TRX and TXNIP involves disulphide bond switching.
From: The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein
(a) TXNIP undergoes disulphide bond switching via a significant Cys63-mediated conformational change. The N-TXNIP structure (yellow) is superimposed onto the T–TXNIP structure (cyan). The interdomain disulphide bond between Cys63 and Cys190 in T–TXNIP and the intramolecular disulphide bond between Cys63 and Cys120 in N-TXNIP are indicated. (b) The interdomain disulphide bond formed between Cys63 of N-TXNIP (magenta) and Cys190 of C-TXNIP (cyan) is located at the centre of the interdomain interface. The residues involved in the interface are depicted using stick representations. The β5, β6, and β14 strands are also indicated. (c) A side-to-side interaction occurs between the TXNIP domains. The interdomain interactions between the N-terminal strand β6 (magenta) and the C-terminal strand β19 (cyan) are shown.
