Author: Gábor Erdos; Bálint Mészáros; Dana Reichmann; Zsuzsanna Dosztányi
Title: Large-scale analysis of redox-sensitive conditionally disordered protein regions reveal their widespread nature and key roles in high-level eukaryotic processes Document date: 2018_9_10
ID: 99m0gt06_19
Snippet: Judging by sheer numbers of occurrence, the most abundant domain of interest in humans is the C2H2 zinc finger. This structural unit is present in all three studied proteomes in high numbers. Furthermore, the ratio of conditionally disordered C2H2 domains compared to the total number of such domains is surprisingly stable across the three organisms, with values of 59.5%, 66.6%, and 53.9%, for yeast, drosophila and human. This indicates that the s.....
Document: Judging by sheer numbers of occurrence, the most abundant domain of interest in humans is the C2H2 zinc finger. This structural unit is present in all three studied proteomes in high numbers. Furthermore, the ratio of conditionally disordered C2H2 domains compared to the total number of such domains is surprisingly stable across the three organisms, with values of 59.5%, 66.6%, and 53.9%, for yeast, drosophila and human. This indicates that the study of the redox-sensitivity of simple model organisms, such as yeast can have implications in human physiology as well. The identification and functional characterization of redox-sensing structural switches can therefore serve as a guide to the understanding of the more complex roles these protein regions play in human regulation.
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