ArticleThe journal of physical chemistry. B2022
Allosteric Inhibition of PTP1B by a Nonpolar Terpenoid.
Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- NMR relaxation dispersion reveals an order of magnitude range of acid loop motions in protein tyrosine phosphatase 1B.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Kinetic Compatibility as a Predictor of PTP1B Inhibitor Combination Outcomes: An Integrated Experimental and Computational Study.ChemMedChem · 2026Article
- Optimization of Indole- and Pyrazole-fused Glycyrrhetinic Acid Derivatives as Potent PTP1B Inhibitors: In Silico, In Vitro, In Vivo, and Metabolomic Studies.ACS bio & med chem Au · 2026Article
- Mechanisms, functions and therapeutic targeting of protein tyrosine phosphatases.Nature reviews. Molecular cell biology · 2026Review
- Dual PTP1B/DPP4 Inhibitory Potential ofComputational and structural biotechnology journal · 2026Article
- False Friends in Fluorescence - Simple HPLC Evaluation of False Positive Fragment Hits in a DiFMUP Assay for Protein Tyrosine Phosphatase 1B.Drug design, development and therapy · 2026Article
- Orchestrating function: Concerted dynamics, allostery, and catalysis in protein tyrosine phosphatases.Current opinion in structural biology · 2025Review
- Review
- Mapping allosteric rewiring in related protein structures from collections of crystallographic multiconformer models.bioRxiv : the preprint server for biology · 2025Article
- Biophysical Rationale for the Selective Inhibition of PTP1B over TCPTP by Nonpolar Terpenoids.The journal of physical chemistry. B · 2023Article
- Analysis of neutral mutational drift in an allosteric enzyme.Protein science : a publication of the Protein Society · 2023Article
- A biophysical rationale for the selective inhibition of PTP1B over TCPTP by nonpolar terpenoids.bioRxiv : the preprint server for biology · 2023Article
- Room-temperature serial synchrotron crystallography of the human phosphatase PTP1B.Acta crystallographica. Section F, Structural biology communications · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein tyrosine phosphatases (PTPs) are promising drug targets for treating a wide range of diseases such as diabetes, cancer, and neurological disorders, but their conserved active sites have complicated the design of selective therapeutics. This study examines the allosteric inhibition of PTP1B by amorphadiene (AD), a terpenoid hydrocarbon that is an unusually selective inhibitor. Molecular dynamics (MD) simulations carried out in this study suggest that AD can stably sample multiple neighboring sites on the allosterically influential C-terminus of the catalytic domain. Binding to these sites requires a disordered α7 helix, which stabilizes the PTP1B-AD complex and may contribute to the selectivity of AD for PTP1B over TCPTP. Intriguingly, the binding mode of AD differs from that of the most well-studied allosteric inhibitor of PTP1B. Indeed, biophysical measurements and MD simulations indicate that the two molecules can bind simultaneously. Upon binding, both inhibitors destabilize the α7 helix by disrupting interactions at the α3-α7 interface and prevent the formation of hydrogen bonds that facilitate closure of the catalytically essential WPD loop. These findings indicate that AD is a promising scaffold for building allosteric inhibitors of PTP1B and illustrate, more broadly, how unfunctionalized terpenoids can engage in specific interactions with protein surfaces.
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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.