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. 2014 Jan 6;5:2958. doi: 10.1038/ncomms3958

Figure 1. Overall structure of the heterodimeric complex of TRX and TXNIP in the asymmetric unit.

Figure 1

(a) Schematic representation of the TXNIP (cyan) and TRX (yellow) constructs used in this study, showing the locations of the cysteines. (b,c) Ribbon representations of the structures of the TRX(C35A)–T–TXNIP(C120S/C170S/C205S/C267S) complex (referred to as Com1) (b) and the TRX(C35A)–T–TXNIP(C170S/C205S/C267S) complex (referred to as Com2) (c). The structures of Com1 and Com2 were determined at resolutions of 2.0 Å and 2.7 Å, respectively. There are two heterodimeric complexes of TRX and TXNIP in the asymmetric unit. The β-sheets and disordered regions of TXNIP are shown in cyan and by white dashed lines, respectively. The α-helices and β-sheets of TRX are shown in yellow. The N-terminal TXNIP (N-TXNIP) and C-terminal TXNIP (C-TXNIP) domains are indicated.