Glutaredoxins (Grxs) comprise a group of glutathione (GSH)-dependent oxidoreductase enzymes that respond to oxidative stress and sustain redox homeostasis. Saccharomyces cerevisiae Grx has a similar interaction patterns through its residues between the residues and the environment. The glutaredoxin domain covers 100% of the entire mature Grx1 and Grx8, while the glutaredoxin domain covers ~ 52% of the entire mature Grx6 and Grx7, which have approximately 74 additional amino acids in their N-terminal regions, whereas Grx3 and Grx4 have two functional domains: glutaredoxin and thioredoxin. We have presented the prediction of disordered regions within these protein sequences. Multiple sequence alignment combined with a phylogenetic tree enabled us to specify the key residues contributing to the differences between Saccharomyces cerevisiae Grxs and the proportion symmetry.
CITATION STYLE
Abdalla, M., Eltayb, W. A., & Yousif, A. (2018, September 3). Comparison of structures among Saccharomyces cerevisiae Grxs proteins. Genes and Environment. BioMed Central Ltd. https://doi.org/10.1186/s41021-018-0104-5
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