ArticleBiochemistry2010
Allosteric regulation of glycogen synthase kinase 3β: a theoretical study.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Targeting the GSK-3β/mTOR axis to overcome chemoresistance in gestational choriocarcinoma: molecular mechanisms and therapeutic opportunities.Cancer chemotherapy and pharmacology · 2026Review
- Estrogen EnhancesBiomolecules · 2024Article
- Understanding Glycogen Synthase Kinase-3: A Novel Avenue for Alzheimer's Disease.Molecular neurobiology · 2024Review
- Rational Design of Dual Inhibitors for Alzheimer's Disease: Insights from Computational Screening of BACE1 and GSK-3β.Current computer-aided drug design · 2024Article
- Crosstalk between GSK-3β-actuated molecular cascades and myocardial physiology.Heart failure reviews · 2021Review
- Microsecond molecular dynamics simulations and dynamic network analysis provide understanding of the allosteric inactivation of GSK3β induced by the L343R mutation.Journal of molecular modeling · 2019Article
- Regulation of platelet-activating factor-induced interleukin-8 expression by protein tyrosine phosphatase 1B.Cell communication and signaling : CCS · 2019Article
- Investigation of naphthofuran moiety as potential dual inhibitor against BACE-1 and GSK-3β: molecular dynamics simulations, binding energy, and network analysis to identify first-in-class dual inhibitors against Alzheimer's disease.Journal of molecular modeling · 2017Article
- Rosetta FlexPepDock web server--high resolution modeling of peptide-protein interactions.Nucleic acids research · 2011Article
- Rosetta FlexPepDock ab-initio: simultaneous folding, docking and refinement of peptides onto their receptors.PloS one · 2011Article
- Deconstructing GSK-3: The Fine Regulation of Its Activity.International journal of Alzheimer's disease · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycogen synthase kinase 3β (GSK-3β) is a serine-threonine kinase belonging to the CMGC family that plays a key role in many biological processes, such as glucose metabolism, cell cycle regulation, and proliferation. Like most protein kinases, GSK-3β is regulated via multiple pathways and sites. We performed all-atom molecular dynamics simulations on the unphosphorylated and phosphorylated unbound GSK-3β and the phosphorylated GSK-3β bound to a peptide substrate, its product, and a derived inhibitor. We found that GSK-3β autophosphorylation at residue Tyr(216) results in widening of the catalytic groove, thereby facilitating substrate access. In addition, we studied the interactions of the phosphorylated GSK-3β with a substrate and peptide inhibitor located at the active site and observed higher affinity of the inhibitor to the kinase. Furthermore, we detected a potential remote binding site which was previously identified in other kinases. In agreement with experiments we observed that binding of specific peptides at this remote site leads to stabilization of the activation loop located in the active site. We speculate that this stabilization could enhance the catalytic activity of the kinase. We point to this remote site as being structurally conserved and suggest that the allosteric phenomenon observed here may occur in the protein kinase superfamily.
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Registered trials
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.