ArticleJournal of the American Chemical Society2008
Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 62 citations in OpenAlex.
- Evaluating Force Matching as a Parametrization Strategy for the CHARMM36m Force Field Using Phosphorylation.The journal of physical chemistry. B · 2026Article
- Structural Dynamics of Protein Interactions Using Site-Directed Spin Labeling of Cysteines to Measure Distances and Rotational Dynamics with EPR Spectroscopy.Applied magnetic resonance · 2024Article
- Charge block-driven liquid-liquid phase separation: A mechanism of how phosphorylation regulates phase behavior of disordered proteins.Biophysics and physicobiology · 2024Review
- Multifunnel Energy Landscapes for Phosphorylated Translation Repressor 4E-BP2 and Its Mutants.Journal of chemical theory and computation · 2020Article
- A hallmark of phospholamban functional divergence is located in the N-terminal phosphorylation domain.Computational and structural biotechnology journal · 2020Article
- Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range.Journal of biomolecular NMR · 2019Article
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- Dynamic anticipation by Cdk2/Cyclin A-bound p27 mediates signal integration in cell cycle regulation.Nature communications · 2019Article
- How phosphorylation influences E1 subunit pyruvate dehydrogenase: A computational study.Scientific reports · 2018Article
- Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex.Biophysical journal · 2017Article
- Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Biophysical reviews · 2017Review
- Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives.European biophysics journal : EBJ · 2016Review
- Deubiquitination and the regulation of stress granule assembly.Current genetics · 2016Review
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
- Functional advantages of dynamic protein disorder.FEBS letters · 2015Review
- Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.Molecular bioSystems · 2015Article
- Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back.Molecular bioSystems · 2015Article
- Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch.Nature · 2015Article
- Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain.Molecular bioSystems · 2014Article
- Structural interrogation of phosphoproteome identified by mass spectrometry reveals allowed and disallowed regions of phosphoconformation.BMC structural biology · 2014Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
We have performed molecular dynamics simulations of the phosphorylation domain (PD) of the regulatory light chain (RLC) of smooth muscle myosin, to gain insight into the thermodynamic principles governing the phosphorylation-induced disorder-to-order transition. Simulations were performed in explicit water under near-physiological conditions, starting with an ideal alpha-helix. In the absence of phosphorylation, the helical periodicity of the peptide was disrupted at residues T9-K11, while phosphorylation significantly favored the helical periodicity, in agreement with experimental data. Using the MM/PBSA approach, we calculated a relative free energy of -7.1 kcal/mol for the disorder-to-order transition. A large enthalpic decrease was compensated by a large loss of conformational entropy, despite the small helical increase (no more than three residues) upon phosphorylation. Phosphorylation decreased the conformational dynamics of K and R side chains, especially R16, which forms a salt bridge with pS19. Mutation of R16 to A or E prevented this phosphorylation-dependent ordering. We propose that phosphorylation balances the enthalpy-entropy compensation of the disorder-to-order transition of RLC via short and long-range electrostatic interactions with positively charged residues of the phosphorylation domain. We suggest that this balance is necessary to induce a disorder-to-order conformational change through a subtle energy switching.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.