ArticleJournal of biological physics2016
Effects of phosphorylation on the intrinsic propensity of backbone conformations of serine/threonine.
Article in Journal of biological physics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A CHK1-mediated phosphorylation switch suppresses human Topoisomerase 1-associated genomic instability.The EMBO journal · 2026Article
- Effects of Phosphorylation on Protein Backbone Dynamics and Conformational Preferences.Journal of chemical theory and computation · 2024Article
- Phosphorylation Induced Conformational Transitions in DNA PolymeraseFrontiers in molecular biosciences · 2022Article
- How Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal.Frontiers in molecular biosciences · 2022Article
- Phosphorylation of CEP83 by TTBK2 is necessary for cilia initiation.The Journal of cell biology · 2019Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Each amino acid has its intrinsic propensity for certain local backbone conformations, which can be further modulated by the physicochemical environment and post-translational modifications. In this work, we study the effects of phosphorylation on the intrinsic propensity for different local backbone conformations of serine/threonine by molecular dynamics simulations. We showed that phosphorylation has very different effects on the intrinsic propensity for certain local backbone conformations for the serine and threonine. The phosphorylation of serine increases the propensity of forming polyproline II, whereas that of threonine has the opposite effect. Detailed analysis showed that such different responses to phosphorylation mainly arise from their different perturbations to the backbone hydration and the geometrical constraints by forming side-chain-backbone hydrogen bonds due to phosphorylation. Such an effect of phosphorylation on backbone conformations can be crucial for understanding the molecular mechanism of phosphorylation-regulated protein structures/dynamics and functions.
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