Protein Domain : Nucleoredoxin, redox inactive TRX-like domain b' IPR041861

Type	Domain
Description	This entry represents the redox inactive TRX-like domain b' found at the C terminus of vertebrate nucleoredoxins (NRX). Despite its name, nucleoredoxins is localized in both the cytosol and the nucleus [ ]. It interacts with phosphofructokinase 1 and protein phosphatase 2A [, ]. It may be involved in transcriptional regulation [] and has been shown to negatively regulate Wnt-beta-catenin signalling and binds to Dvl (Dishevelled) in a redox-dependent manner []. The mouse NRX gene is implicated in streptozotocin-induced diabetes []. The NRX protein contains three TRX domains organized in a structure similar to those of PDIs that contain three to four TRX domains. The N- and C-terminal domains of NRX share a high similarity to the b' domains of PDIs and lack a redox active centre. The central domain, however, contains the dithiol active site motif Cys-Pro-Pro-Cys and was shown to be active in the insulin reduction assay. The function of the PDI-like domains in NRX is unclear; they may be important for substrate recognition [].Thioredoxin family members are evolutionary conserved proteins that possess catalytically active cysteine residues that can reduce the disulphide bonds of target proteins. Thioredoxin family members include nucleoredoxins (NRX), Trxs, glutaredoxins (Grxs), peroxiredoxins (Prxs), and protein disulfide isomerases (PDIs) that catalyze cellular redox signaling [ ]. Thioredoxin possesses a conserved WCGPC (Trp-Cys-Gly-Pro-Cys) motif, and the two cysteine residues (Cys32 and Cys35 in human TRX1) are directly involved in oxidoreductase reactivity [].
Short Name	NRX_PDI_b'