Thioredoxin fold domain-containing protein
Webcollagen, 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 WebRelevant bibliographies by topics / Thioredoxin domain containing protein 5. Academic literature on the topic 'Thioredoxin domain containing protein 5' Author: Grafiati. Published: 4 June 2024 Last updated: 16 February 2024 Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles ...
Thioredoxin fold domain-containing protein
Did you know?
WebOct 23, 2009 · The protein domain structure within the Trx fold class is varied and modular. Analysis of these sequences indicates that while most members contain just one copy of a certain thioredoxin fold domain embedded in the protein-coding sequence, some classes … WebDec 1, 2024 · Besides TXNDC5, a total of more than 20 PDI family members have been identified in human cells. 5 As a common structural feature, all members of the PDI family contain one or more of the thioredoxin-like domain that consists of the signature sequence cysteine-X-X-cysteine (CXXC). The existence of multiple PDI members in mammalian cells …
The 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 protein fold that has oxidoreductase activity. … See more Despite sequence variability in many regions of the fold, thioredoxin proteins share a common active site sequence with two reactive cysteine residues: Cys-X-Y-Cys, where X and Y are often but not necessarily See more Different thioredoxin fold-containing proteins vary greatly in their reactivity and in the pKa of their free thiols, which derives from the ability of the overall protein structure to stabilize the activated thiolate. Although the structure is fairly consistent among proteins … See more • SCOP thioredoxin superfamily • CATH glutaredoxin topology See more Human proteins containing this domain include: • DNAJC10 • ERP70 • GLRX3 • P4HB; PDIA2; PDIA3; PDIA4; PDIA5; PDIA6 (P5); PDILT See more WebNov 6, 2012 · The S2 pockets (Figure 3A–C) are cavities present in the thioredoxin-like folds of each domain, and are comparatively smaller than the S1 pocket. Although there are three S2 pockets, one located in the thioredoxin-like fold in each of the three domains, they displayed significant variations in size and surface charge due to variations in ...
WebSep 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. ... WebMar 8, 2013 · Thioredoxin-interacting protein (TxNIP) is up-regulated by high glucose and is associated with oxidative stress. It has been implicated in hyperglycemia-induced β-cell dysfunction and apoptosis. As high glucose and oxidative stress mediate diabetic nephropathy (DN), the contribution of TxNIP was investigated in renal mesangial cell …
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 …
WebMar 8, 2024 · The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox … rabbit movies freeWebSusumu 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 … rabbit mp3 musicWebJun 2, 2024 · The mammalian cytosolic thioredoxin (Trx) system consists of Trx1 and its reductase, the NADPH-dependent seleno-enzyme TrxR1. These proteins function as electron donor for metabolic enzymes, for instance in DNA synthesis, and the redox regulation of numerous processes. In this work, we analysed the interactions between these two … rabbit moving and storageWebSusumu 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 located in the N-terminus of a long kinked helix that spans the length of the protein (Rowe et al., 2009). rabbit moving companyWebThe 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 … shoalhaven radiation oncologyWebThioredoxin-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. … shoalhaven railingsWebFeb 23, 2024 · Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low Km for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin suggest that TSTD1 might play a role in sulfide-based signaling. shoalhaven real estate