ArticleScientific reports2015
Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Mechanisms of systolic heart failure in PP2CxPP5 double transgenic mice.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- The Inhibition of Serine/Threonine Protein Phosphatase Type 5 Mediates Cantharidin Toxicity to ControlInsects · 2020Article
- Structural dynamic studies on identification of EGCG analogues for the inhibition of Human Papillomavirus E7.Scientific reports · 2020Article
- Review: Precision medicine and driver mutations: Computational methods, functional assays and conformational principles for interpreting cancer drivers.PLoS computational biology · 2019Review
- Interactions of cantharidin-like inhibitors with human protein phosphatase-5 in a MgJournal of molecular modeling · 2018Article
- Article
- Molecular Dynamics Simulations and Dynamic Network Analysis Reveal the Allosteric Unbinding of Monobody to H-Ras Triggered by R135K Mutation.International journal of molecular sciences · 2017Article
- Structure-based discovery of potentially active semiochemicals for Cydia pomonella (L.).Scientific reports · 2016Article
- Structural insights into Cydia pomonella pheromone binding protein 2 mediated prediction of potentially active semiochemicals.Scientific reports · 2016Article
- The Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B.Scientific reports · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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Abstract
Serine/threonine protein phosphatase 5 (PP5) is a promising novel target for anticancer therapies. This work aims to uncover the key interactions at the atomic level between PP5 and three inhibitors (cantharidin, norcantharidin and endothall). We found that, unlike previous report, Arg 100 contributes less to PP5-inhibitor binding, and the residues His 69, Asn 128, His 129, Arg 225, His 252 and Arg 250 are of importance to PP5-inhibitor binding. The hydrophobic interactions established between the residues Val 254, Phe 271 and Tyr 276, especially Glu 253, are very important to enhance the inhibitive interaction. We suggested that, to increase the inhibitory activity, the interactions of inhibitor with three negatively charged unfavorable interaction residues, Asp 99, Glu 130 and Asp 213, should be avoided. However, the interactions of inhibitor with favorable interaction residue Arg 250 could enhance the inhibitory activity. The Manganese ion 2 (MN2) unfavorably contribute to the total interaction free energies. The coordination between MN2 and chemical group of inhibitor should be eliminated. This work provides insight into how cantharidin and its analogs bind to PP5c at the atomic level and will facilitate modification of cantharidin-like chemicals to rationally develop more specific and less cytotoxic anti-cancer drugs.
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