Figure 5: N-TXNIP undergoes a Cys63-mediated conformational change.
From: The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein
(a) Ribbon representation of N-TXNIP showing the intramolecular disulphide bond between Cys63 and Cys120. The locations of other cysteine residues are also shown. (b) N-TXNIP structures were superimposed onto the N-TXNIP(K5A/K6A) structure (grey). The structure of N-TXNIP(C36S/C49S/K64A/C120S) (Protein Data Bank accession code 4GEI) is shown in yellow. The structures of the crystallographically independent molecules of N-TXNIP(C36S/C49S/C120S) (Protein Data Bank accession code 4GEJ) are shown in different colours. The N-terminal domain of Com1 (red) has a similar conformation to the D-chain structure (wheat) of N-TXNIP(C36S/C49S/C120S). The region that undergoes significant structural changes between the N-TXNIP structures is indicated by the black dashed line box. The locations of the Cys63, Cys120 and Ser120 residues are indicated.
