ArticleBiophysical journal2011
Modeling the binding of three toxins to the voltage-gated potassium channel (Kv1.3).
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- Inhibitory Effects of 2-Aminoethoxydiphenyl Borate (2-APB) on Three KMolecules (Basel, Switzerland) · 2023Article
- Design of New Potent and Selective Thiophene-Based KCancers · 2022Article
- Genomic Structure of Two Kv1.3 Channel Blockers from Scorpion Mesobuthus eupeus and Sea Anemone Stichodactyla haddoni and Construction of their Chimeric Peptide as a Novel Blocker.Biochemical genetics · 2022Article
- Discovery of KMedicinal research reviews · 2021Review
- Conformational exchange in the potassium channel blocker ShK.Scientific reports · 2019Article
- Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes.Molecules (Basel, Switzerland) · 2019Review
- Centipede KCNQ Inhibitor SsTx Also Targets KToxins · 2019Article
- Scorpion toxins targeting Kv1.3 channels: insights into immunosuppression.The journal of venomous animals and toxins including tropical diseases · 2019Article
- Article
- Molecular Dynamics Simulation Reveals Specific Interaction Sites between Scorpion Toxins and KToxins · 2017Article
- Molecular Simulations of Disulfide-Rich Venom Peptides with Ion Channels and Membranes.Molecules (Basel, Switzerland) · 2017Review
- Margatoxin-bound quantum dots as a novel inhibitor of the voltage-gated ion channel Kv1.3.Journal of neurochemistry · 2017Article
- T Cell Subset and Stimulation Strength-Dependent Modulation of T Cell Activation by Kv1.3 Blockers.PloS one · 2017Article
- Article
- Article
- Review
- Scorpion toxins prefer salt solutions.Journal of molecular modeling · 2015Article
- A single conserved basic residue in the potassium channel filter region controls KCNQ1 insensitivity toward scorpion toxins.Biochemistry and biophysics reports · 2015Article
- Article
- Computational approaches for designing potent and selective analogs of peptide toxins as novel therapeutics.Future medicinal chemistry · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conduction properties of the voltage-gated potassium channel Kv1.3 and its modes of interaction with several polypeptide venoms are examined using Brownian dynamics simulations and molecular dynamics calculations. Employing an open-state homology model of Kv1.3, we first determine current-voltage and current-concentration curves and ascertain that simulated results accord with experimental measurements. We then investigate, using a molecular docking method and molecular dynamics simulations, the complexes formed between the Kv1.3 channel and several Kv-specific polypeptide toxins that are known to interfere with the conducting mechanisms of several classes of voltage-gated K(+) channels. The depths of potential of mean force encountered by charybdotoxin, α-KTx3.7 (also known as OSK1) and ShK are, respectively, -19, -27, and -25 kT. The dissociation constants calculated from the profiles of potential of mean force correspond closely to the experimentally determined values. We pinpoint the residues in the toxins and the channel that are critical for the formation of the stable venom-channel complexes.
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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.