ArticleAnnals of translational medicine2022
Homology modeling and molecular docking simulation of martentoxin as a specific inhibitor of the BK channel.
Article in Annals of translational medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Reproducibility, validation, and failure modes across classical and AI-driven molecular docking.Journal of computer-aided molecular design · 2026Review
- Exploring the Therapeutic Potential ofInternational journal of molecular sciences · 2025Article
- The Significant Therapeutic Effects of Chinese Scorpion: Modern Scientific Exploration of Ion Channels.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Machine Learning-Based Virtual Screening and Molecular Simulation Approaches Identified Novel Potential Inhibitors for Cancer Therapy.Biomedicines · 2023Article
- The toxic natural product tutin causes epileptic seizures in mice by activating calcineurin.Signal transduction and targeted therapy · 2023Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Large conductance calcium-activated potassium channel (BK channel) is gated by both voltage and calcium ions and is widely distributed in excitable and nonexcitable cells. BK channel plays an important role in epilepsy and other diseases, but BK channel subtype-specific drugs are still extremely rare. Martentoxin was previously isolated from the venom of members of Scorpionidae and shown to be composed of 37 amino acids. Research has shown that the pharmacological selectivity of martentoxin to the BK channel is higher than that to other potassium channels. Therefore, it is of great significance to study the mechanism of interaction between martentoxin and BK channels. Methods: The three-dimensional structure of BK channel pore region was constructed by homologous modeling method, and the key amino acid sites of BK channel interaction with martentoxin were analyzed by protein-protein docking, molecular dynamic simulation and virtual alanine mutation. Results: Based on homologous modeling of BK channel pore structure and protein-protein docking analysis, Phe1, Lys28 and Arg35 of martentoxin were found to be key amino acids in toxin BK channel interaction. Conclusions: This study reveals the structural basis of martentoxin interaction with BK channel. These results will contribute to the design of BK channel specific blockers based on the structure of martentoxin.
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