Thioredoxin fold domain-containing protein
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 … WebMar 1, 1995 · The thioredoxin fold, named after the protein in which it was first observed, is a distinct structural motif consisting of a four-stranded β -sheet and three flanking α -helices. It has been identified in the three-dimensional structures of proteins from five classes: …
Thioredoxin fold domain-containing protein
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WebFeb 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. 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 evolution, the assembly of different Trx fold domains has been used ...
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 … WebMar 29, 2024 · thioredoxin domain containing 15 provided by HGNC Primary source HGNC:HGNC:20652 See related Ensembl:ENSG00000113621 MIM:617778; AllianceGenome:HGNC:20652 Gene type protein coding RefSeq status REVIEWED …
WebJan 10, 2003 · A complex array of chaperones and enzymes reside in the endoplasmic reticulum (ER) to assist the folding and assembly of and the disulfide bond formation in nascent secretory proteins. Here we characterize a novel human putative ER co-chaperone (ERdj5) containing domains resembling DnaJ, protein-disulfide isomerase, and … WebJun 1, 2003 · Two novel proteins, thioredoxin domain-containing protein 5 (TXNDC5) upregulated in varioliform gastritis, and neuropolypeptide h3 [phosphatidylethanolamine-binding protein 1 (PEBP1 ...
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
WebApr 14, 2024 · In fact, several proteins in the cyanobacterial cytoplasm contain disulfide bridges, and the (in part reversible) formation of disulfide bridges is mediated by the thioredoxin system 68,69,70. tax cottage yucaipaWebSep 28, 2024 · As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found … the cheek in spanishWebRelevant 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 ... taxcountWebThioredoxin-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. … the cheekbone is called theWebSep 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. ... taxcounting s.r.oWebSep 22, 2024 · This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. [provided by RefSeq, Apr 2024] Other designations. thioredoxin domain-containing protein 15, 2310047H23Rik, disulfide … the cheeks are thinWebThe group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the variation in catalytic machinery of Trx fold proteins is essential in providing a foundation for understanding their functional diversity and predicting the function of the many uncharacterized members … the cheek of night