ArticleInternational journal of molecular sciences2014
Insight into conformational change for 14-3-3σ protein by molecular dynamics simulation.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Hydrogen-Deuterium Exchange Mass Spectrometry for Molecular Glue Characterization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Deciphering opening mechanisms of 14-3-3 proteins.Protein science : a publication of the Protein Society · 2025Article
- Physiological Consequences of Targeting 14-3-3 and Its Interacting Partners in Neurodegenerative Diseases.International journal of molecular sciences · 2022Article
- In Silico Studies on GCP-Lys-OMe as a Potential 14-3-3σ Homodimer Stabilizer.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Crystal structure of potato 14-3-3 protein St14f revealed the importance of helix I in StFDL1 recognition.Scientific reports · 2022Article
- Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration.Metabolic brain disease · 2022Review
- 14-3-3σ and Its Modulators in Cancer.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Article
- Atomistic Analysis of ToxN and ToxI Complex Unbinding Mechanism.International journal of molecular sciences · 2018Article
- Free energy calculations on the stability of the 14-3-3ζ protein.Biochimica et biophysica acta. Proteins and proteomics · 2018Article
- Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners.Scientific reports · 2017Article
- Article
- Revealing the binding modes and the unbinding of 14-3-3σ proteins and inhibitors by computational methods.Scientific reports · 2015Article
- Conformational stability of PCID2 upon DSS1 binding with molecular dynamics simulation.Journal of molecular modeling · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
14-3-3σ is a member of a highly conserved family of 14-3-3 proteins that has a double-edged sword role in human cancers. Former reports have indicated that the 14-3-3 protein may be in an open or closed state. In this work, we found that the apo-14-3-3σ is in an open state compared with the phosphopeptide bound 14-3-3σ complex which is in a more closed state based on our 80 ns molecular dynamics (MD) simulations. The interaction between the two monomers of 14-3-3σ in the open state is the same as that in the closed state. In both open and closed states, helices A to D, which are involved in dimerization, are stable. However, large differences are found in helices E and F. The hydrophobic contacts and hydrogen bonds between helices E and G in apo-14-3-3σ are different from those in the bound 14-3-3σ complex. The restrained and the mutated (Arg56 or Arg129 to alanine) MD simulations indicate that the conformation of four residues (Lys49, Arg56, Arg129 and Tyr130) may play an important role to keep the 14-3-3σ protein in an open or closed state. These results would be useful to evaluate the 14-3-3σ protein structure-function relationship.
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