Thioredoxin fold domain-containing protein
Thioredoxin is a 12-kD oxidoreductase protein. Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce other proteins. For Trx1, this process begins by attack of Cys32, one of the residues conserve… Thioredoxin is a 12-kD oxidoreductase protein. Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce other proteins. For Trx1, this process begins by attack of Cys32, one of the residues conserve… WebThioredoxin-like fold domain-containing protein InterPro annotation. Gene names. Ordered locus names. DP0946 Imported. Organism names. Organism. Desulfotalea psychrophila (strain LSv54 / DSM 12343) Imported. ... Protein-protein interaction databases. STRING. …
Thioredoxin fold domain-containing protein
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WebMar 10, 2024 · Thioredoxin (TRX) fold proteins (TFP) are a family of diverse proteins that possess a common domain consisting of four stranded beta-sheets flanked by three alpha-helices, and the redox-active CXXC motif [].The most representative member of this family is thioredoxin, a small disulfide reductase that helps to maintain a reducing cytosolic … WebThe Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During …
WebQuiescin sulfhydryl oxidase 1 (QSOX1), a catalyst of disulfide bond formation secreted by fibroblasts, is a multi‐domain thioredoxin … WebJul 5, 2005 · Thioredoxin domain-containing protein 11. Gene. TXNDC11. Status. UniProtKB reviewed (Swiss-Prot) Organism. Homo sapiens (Human) Amino acids. 985. ... Function. function. May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the …
WebThe thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical example thioredoxin and is found in both prokaryotic and eukaryotic proteins. It is an example of an alpha/beta … WebAbstract: Thioredoxin fold proteins (TFPs) form a family of diverse proteins involved in thiol/disulfide ... are a family of diverse proteins that possess a common domain consisting of four stranded beta-sheets flanked by three alpha-helices, and the redox-active CXXC motif [1]. The most representative member of this family is thioredoxin, a ...
WebMar 1, 1995 · The thioredoxin fold in situ. The thioredoxin fold comprises about 80 residues, but each of the proteins containing it has extra residues in addition to the fold (Figure 1).Glutaredoxin (87 residues) and thioredoxin (108 residues) are single-domain monomeric proteins: glutaredoxin has little structure in addition to the basic thioredoxin fold, whereas …
WebJun 4, 2024 · Two of the 3 most highly up-regulated genes were tumor suppressor genes, that is, thioredoxin-interacting protein (TXNIP; 3.7-fold) and zinc finger and BTB domain containing 16 (ZBTB16; 8.8-fold). About 50% of the differentially expressed genes were functionally categorized in 3 major routes, namely MAPK pathways (9 genes), NF-κB … portland trick or treating 2022WebThioredoxin domain containing 5 (TXNDC5), an ER-localized protein disulfide isomerase, was shown to facilitate ECM protein folding and to contribute to the stability of ECM proteins. Enhanced expression of TXNDC5 promoted redox-sensitive activation of cardiac … portland trimetWebSusumu Imaoka, in International Review of Cell and Molecular Biology, 2011. 3.6 ERp18. ERp18 is the smallest member of the PDI family to contain a CXXC motif. Like the catalytic domains of PDI, ERp18 adopts a thioredoxin fold with a thioredoxin-like active site … portland trick or treat 2022WebFeb 23, 2024 · TSTD1 also shares a similar fold with other rhodanese domain–containing proteins. However, some minor differences are observed. TSTD1 displays shorter helices, namely α2, α4, and α6, compared with RDL1 (Fig. 2, A and B) (19). Another point of difference is the presence of an additional α-helix, α3, in TSTD1, which is absent in RLD1. option for the poor and vulnerable meaningWebApr 11, 2003 · protein folding Source:GO_Central. 1 publication. Expand table. Complete GO annotation on QuickGO ... Thioredoxin domain-containing protein 5 By similarity. EC number. EC:1.8.4.- ... names. Endoplasmic reticulum resident protein 46 By similarity (ER … option for the poor and vulnerable usccbWebSep 19, 2024 · disintegrin and metalloproteinase domain-containing protein 10: 3.24: 1.7: 21.76: 2.75 × 10 −3: ... Proteins with the highest fold changes observed over the course of the MLR, ... ERp5 and ERp57, contain thioredoxin-like domains, it is possible that they are also inhibited. Similar effects were observed by Lawrence et al. ... portland trimet taxWebcollagen, connective tissue, cartilagen, tendons, etc.; 2) labile compounds and non-protein-bound thiols, such as glutathione (GSH); and 3) the muscle mass. Figure 1. Methionine/glutathione transsulfuration pathway. Methionine is converted by methionine adenosyltransferase to S-adenosylmethionine, which is then converted to portland trimet bus