The Thioredoxin (Trx) system plays important roles in several diseases (e.g. cancer, viral infections, cardiovascular and neurodegenerative diseases). Therefore, there is a therapeutic interest in the design of modulators of this system. In this work, we used normal mode analysis to identify putative binding site regions for Human Trx1 that arise from global motions. We identified three possible inhibitor's binding regions that corroborate previous experimental findings. We show that intrinsic motions of the protein are related to the exposure of hydrophobic regions and non-active site cysteines that could constitute new binding sites for inhibitors.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.jsb.2013.09.002 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Transcriptome and translatome profiling of Col-0 and grp7grp8 under ABA treatment in Arabidopsis.
Sci Data
December 2024
Key Laboratory of Plant Cell and Chromosome Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.
Abscisic acid (ABA) is a crucial phytohormone that regulates plant growth and stress responses. While substantial knowledge exists about transcriptional regulation, the molecular mechanisms underlying ABA-triggered translational regulation remain unclear. Recent advances in deep sequencing of ribosome footprints (Ribo-seq) enable the mapping and quantification of mRNA translation efficiency.
View Article and Find Full Text PDFModeling and interaction study of alcohol oxidase and ProteaseA in methylotrophic yeast : insights from In-silico analysis.
J Biomol Struct Dyn
December 2024
Department of Bioinformatics, School of Life Sciences Pondicherry University, Puducherry, India.
Flavin adenine nucleotide (FAD)-dependent oxidoreductase enzyme Alcohol oxidase (AOX) facilitates the growth of methylotrophic yeast C. boidinii by catabolizing methanol, producing formaldehyde and hydrogen peroxide. Vacuolar Protease-A (PrA) from C.
View Article and Find Full Text PDFIdentification of the arachidonic acid 5-lipoxygenase and its function in the immunity of Apostichopus japonicus.
Fish Shellfish Immunol
December 2024
Department of Biotechnology, School of Biological Engineering, Dalian Polytechnic University, Dalian 116034, Liaoning Province, P. R. China; Dalian Jinshiwan Laboratory, Dalian, China. Electronic address:
A number of studies have been demonstrated that arachidonate 5-lipoxygenase (ALOX-5) plays a role in regulating a range of physiological and pathological processes through the catalysis of leukotriene formation from arachidonic acid (ARA). The coding sequence of ALOX-5 from Apostichopus japonicus (Aj-ALOX-5) was successfully amplified, resulting in a 2028 bp ORF sequence that encodes 674 amino acids. A comparison of the amino acid sequence with those of other 5-lipoxygenases revealed that Aj-ALOX-5 has the N-terminal "PLAT domain" and C-terminal "lipoxygenase structural domain" characteristic of this enzyme family.
View Article and Find Full Text PDFEffects of molecular weight of chitosan on its binding ability with OSA starch and oil-water interface behavior of complex-stabilized emulsion.
Int J Biol Macromol
December 2024
School of Agriculture, Food and Ecosystem Sciences, Faculty of Science, The University of Melbourne, Parkville, Vic 3010, Australia. Electronic address:
This work examined the effects of molecular weight (2-15 kDa) and concentration (10-30 mg/mL) of chitosan (CTS) on the binding capacity and interface behavior between octenyl succinic acid sodium starch (OSS) and CTS, as well as their effects on the storage stability of emulsions. The results of the isothermal calorimetry titration demonstrated that OSS and CTS were complexed by electrostatic interaction and spontaneous hydrogen bonding driven by enthalpy (ΔH from -3931 to -7983 cal/mol, ΔS from -38.5 to -49.
View Article and Find Full Text PDFA crucial active site network of titratable residues guides catalysis and NAD binding in human succinic semialdehyde dehydrogenase.
Protein Sci
January 2025
Department of Neuroscience, Biomedicine and Movement Sciences, Section of Biochemistry, University of Verona, Verona, Italy.
Human succinic semialdehyde dehydrogenase is a mitochondrial enzyme fundamental in the neurotransmitter γ-aminobutyric acid catabolism. It catalyzes the NAD-dependent oxidative degradation of its derivative, succinic semialdehyde, to succinic acid. Mutations in its gene lead to an inherited neurometabolic rare disease, succinic semialdehyde dehydrogenase deficiency, characterized by mental and developmental delay.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!