Thioredoxin fold domain containing protein
Web21 rows · Thioredoxin domain containing 5 (TXNDC5), an ER-localized protein disulfide isomerase, was ... WebDec 25, 2001 · There is a large superfamily of proteins that contain one or multiple thioredoxin domains . Such proteins containing a thioredoxin fold are found in all organisms and can be grouped into at least six classes: thioredoxins, glutaredoxins, DsbA, protein disulfide isomerase, glutathione transferases, and glutathione peroxidases [ 40,41 ].
Thioredoxin fold domain containing protein
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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 Human proteins containing this domain include: • DNAJC10 • ERP70 • GLRX3 See more • SCOP thioredoxin superfamily • CATH glutaredoxin topology See more WebJun 1, 2003 · Two novel proteins, thioredoxin domain-containing protein 5 (TXNDC5) upregulated in varioliform gastritis, and neuropolypeptide h3 [phosphatidylethanolamine …
WebApr 11, 2003 · protein folding Source:GO_Central. 1 publication. Expand table. Complete GO annotation on QuickGO ... Thioredoxin domain-containing protein 5 By similarity. EC … 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 ...
WebJun 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 … WebFeb 5, 2024 · thioredoxin domain containing 16 provided by HGNC Primary source HGNC:HGNC:19965 See related Ensembl:ENSG00000087301 MIM:616179; …
WebRelevant bibliographies by topics / Thioredoxin domain containing protein 5. Academic literature on the topic 'Thioredoxin domain containing protein 5' Author: Grafiati. …
WebThioredoxin-like fold domain-containing protein MRL7L, chloroplastic Curated. Alternative names. Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7-LIKE 1 publication ... Thioredoxin-like fold domain-containing protein MRL7L, chloroplastic: BLAST Add. Sequence: Expand table. Proteomic databases. PaxDb. Q9SKB6; ProteomicsDB. 250861; PTM databases. … jobs ipswich suffolkThioredoxins are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulfide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. The net result is the covalent interconversion of a disulfide and a dithiol. int 1871 inovation speakersWebFeb 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. int 1871 innovation speakersWebMar 14, 2024 · Background: Proteins with a thioredoxin (Trx) fold share several structural features but carry out different reactions.Results: The contribution of the electrostatic environment of the active site to the reactivity of Trx-fold proteins is described.Conclusion: Function and reactivity of the Trx fold depend on an extended active-site … jobsireland trainingWebMar 29, 2024 · This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide … jobs ireland community employmentWebThioredoxins[1][2][3][4] are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulfide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulfide, accompanied by the transfer … jobs in zurich airport for english speakerWebThioredoxin - a fold for all reasons The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common … jobs ipswich hospital nhs trust