Thioredoxin-like fold protein
WebMar 29, 2024 · The ability of thioredoxin, a protein disulfide isomerase (PDI), to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 gp120 and thioredoxin also … WebApr 13, 2024 · HIGHLIGHTS. who: Sadek Amhaz from the (UNIVERSITY) have published the article: The UAS thioredoxin-like domain of UBXN7 regulates E3 ubiquitin ligase activity of RNF111/Arkadia, in the Journal: (JOURNAL) what: The authors have identified UBXN7 as a direct regulator of RNF111. Noticeably, the authors provide evidence that, unlike RNF111, …
Thioredoxin-like fold protein
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WebApr 14, 2024 · In addition, the mutant protein seemed to be correctly folded at the secondary structure level as indicated by circular dichroism (CD) spectra of SynDLP wt and SynDLP C777A, which were identical ... 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 …
WebJan 23, 2004 · On the basis of sequence analysis, more than 1000 proteins have been proposed to contain a redox-active Cys-X-X-Cys motif in a thioredoxin-like fold ( 27 ). Most of these proteins are believed to carry out the oxidation, reduction, or isomerization of substrate proteins via formation of mixed disulfide complexes ( 2, 3 ). Webdoxin-like fold. We employ this definition of the thioredoxin-like fold to query the PDB database using a protein structure motif search program (unpublished). Identified …
WebFeb 1, 2005 · We define the thioredoxin-like fold using the structure consensus of thioredoxin homologs and consider all circular permutations of the fold. The search for … WebJun 11, 2007 · The Dim protein family is composed of two classes, Dim1 and Dim2, which share a common thioredoxin-like fold. They were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP.
WebHere, one thioredoxin-like fold protein, Arabidopsis early chloroplast biogenesis 1 (AtECB1), an allele of MRL7, was identified to regulate PEP function and chloroplast biogenesis. The knockout lines for AtECB1 displayed albino phenotype and impaired chloroplast development. The transcripts of PEP-dependent plastid genes were barely detected ...
WebMar 1, 1995 · The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common property of interacting with cysteine-containing substrates. ... Cytochrome c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein. Proc. Natl. Acad. Sci. USA, 90 ... toothache medicationWebJan 16, 2024 · Thioredoxin-interacting protein (TXNIP) plays a critical role in cellular redox control by thioredoxin. TXNIP serves as a glucose and oxidative stress sensor, being commonly silenced by genetic or epigenetic events in cancer cells. physiotherapie westend münchenWebJan 15, 2004 · Immunoglobulin-like fold; Immunoglobulin-like domain; Thioredoxin; Thioredoxin-like superfamily; Structure domains: V set domains (antibody variable domain-like) ... Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Haste Andersen et al. (2006) 10 more tooth ache in pregnancyhttp://prodata.swmed.edu/Lab/Thiored_Proteins04.pdf physiotherapie wesseling am rheinWebJan 1, 2014 · Since AtECB1 is annotated as a thioredoxin-like fold protein and contains a typical βαβαββα structure of thioredoxins, we investigated whether the protein harbors … toothache making ear hurtWebThioredoxin 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. physiotherapie wien 1050 alle kassenThioredoxin 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… physiotherapie wien 1030 alle kassen