ArticleStructure (London, England : 1993)2015
Two pathways mediate interdomain allosteric regulation in pin1.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Residue Interaction Network Reveals Allosteric Pathways Linking Orthosteric and Intracellular Sites in Class A GPCRs.Journal of chemical information and modeling · 2026Article
- Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions Using an Integrated Mass Spectrometry Approach.ACS chemical biology · 2026Article
- AlloViz: A tool for the calculation and visualisation of protein allosteric communication networks.Computational and structural biotechnology journal · 2024Article
- Dissecting Allosteric Mutations for Antibiotic Resistance by Time-Dependent Linear Response Theory.Journal of chemical theory and computation · 2024Article
- Article
- Article
- Exploring the molecular mechanism of cold-adaption of an alkaline protease mutant by molecular dynamics simulations and residue interaction network.Protein science : a publication of the Protein Society · 2023Article
- Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.Advances in biological regulation · 2023Article
- Ligand-specific conformational change drives interdomain allostery in Pin1.Nature communications · 2022Article
- Neural relational inference to learn long-range allosteric interactions in proteins from molecular dynamics simulations.Nature communications · 2022Article
- Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.Journal of the American Chemical Society · 2021Article
- Substitutions at Nonconserved Rheostat Positions Modulate Function by Rewiring Long-Range, Dynamic Interactions.Molecular biology and evolution · 2021Article
- Protein Allostery at Atomic Resolution.Angewandte Chemie (International ed. in English) · 2020Article
- Allostery and Epistasis: Emergent Properties of Anisotropic Networks.Entropy (Basel, Switzerland) · 2020Article
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
- PIN1 Provides Dynamic Control of MYC in Response to Extrinsic Signals.Frontiers in cell and developmental biology · 2020Article
- Review
- Allostery in Its Many Disguises: From Theory to Applications.Structure (London, England : 1993) · 2019Review
- Molecular Mechanism of the Pin1-Histone H1 Interaction.Biochemistry · 2019Article
- Mutational effects of Cys113 on structural dynamics of Pin1.Biophysics and physicobiology · 2019Article
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3 authors.
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Abstract
Allostery is an essential means for regulating biomolecular functions and provides unique opportunities for drug design, yet our ability to elucidate allosteric mechanisms remains limited. Here, based on extensive molecular dynamics simulations, we present an atomistic picture of the pathways mediating the allosteric regulation of the PPIase domain of Pin1 by its WW domain. Two pathways jointly propagate the action of substrate-WW binding to produce closure and rigidification of three PPIase catalytic-site loops. One pathway preexists in the apo protein, but remains dormant until substrate-WW binding completes the second. The reduction in conformational entropy and preorganization of the catalytic-site loops observed here may explain why substrate-WW binding enhances ligand affinity and catalytic activity of the PPIase domain and suggest a combination drug therapy for Pin1-related diseases. Whereas the traditional view of allostery has emphasized conformational transition, our study identifies a distinct role of conformational dynamics in eliciting allostery.
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