Thioredoxin-like fold protein
WebJan 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. WebApr 1, 2008 · In the catalytic mechanism thioredoxin fold proteins bind to target proteins through conserved backbone–backbone hydrogen bonds and induce conformational changes of the target disulfide followed by nucleophilic attack by the N-terminally located low p Keywords Protein disulfide 1. Introduction
Thioredoxin-like fold protein
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WebApr 14, 2024 · Recombinant protein production and purification. The GDAP1Δ303–358 and GDAP1Δ319–358 constructs, with an N-terminal His 6 tag and a Tobacco Etch Virus (TEV) protease digestion site, for producing soluble recombinant human GDAP1 in E. coli, have been described [].The point mutations R120Q, R161H, A247V, H256R, and R282H were … 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 …
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this definition of the thioredoxin-like fold to query the PDB database using a protein structure motif search program (unpublished).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 … 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. The fold's spatial topology consists of a four-stranded antiparallel beta sheet sandwiched …
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 … 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 [ 1 ].
WebAll members of the PDI family share the thioredoxin-like domain structure characterized by the βαβαβαββα fold (Kemmink et al., 1997). PDI contains four thioredoxin-like domains abb'a'. The two redox active sites containing the CXXC motif are found in the a and a' domains (Figure 2). The active site domains are linked by the b and b ...
WebThioredoxin - 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 property of interacting with cysteine-containing substrates. Structure 15 March 1995, 3:245-250 The thioredoxin fold, named after the protein in which ordinal hlaWebThioredoxin 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. how to turn a browser tax form into a pdfWebMar 8, 2013 · Thioredoxin-interacting protein (TxNIP) is up-regulated by high glucose and is associated with oxidative stress. ... After 3 h of HG exposure there was a 2.3 ± 0.16-fold increase in superoxide production in C3H MC that remained higher at 24 h. In contrast, ... a Warburg-like effect . how to turn a candle holder on a latheWebJun 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. how to turn a camera in tabsWebSep 16, 2016 · Similar to many other selenoproteins, SEP15 belongs to the class of thiol- oxidoreductases [5, 9].It contains a thioredoxin-like fold [], with selenocysteine located in the predicted catalytic position, and also contains an ER-targeting signaling peptide in the N-terminal region (Fig. 19.1b) [].The structure of its thioredoxin-like domain, as shown by … ordinal identifiers in uftWebStructure. Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import … how to turn a canva presentation into a pdfWebJan 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 how to turn a cartwheel into a backflip