ArticleBMC structural biology2007
Monte Carlo-energy minimization of correolide in the Kv1.3 channel: possible role of potassium ion in ligand-receptor interactions.
Article in BMC structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 27 citations in OpenAlex.
- Design and synthesis of novel small molecules targeting the Kv1.3 voltage-gated potassium ion channel.Scientific reports · 2025Article
- Energy for wild-type acetylcholine receptor channel gating from different choline derivatives.Biophysical journal · 2013Article
- Structure-activity relationship exploration of Kv1.3 blockers based on diphenoxylate.Bioorganic & medicinal chemistry letters · 2012Article
- A specific two-pore domain potassium channel blocker defines the structure of the TASK-1 open pore.The Journal of biological chemistry · 2011Article
- Overlapping binding sites of structurally different antiarrhythmics flecainide and propafenone in the subunit interface of potassium channel Kv2.1.The Journal of biological chemistry · 2010Article
- Potassium channel block by a tripartite complex of two cationophilic ligands and a potassium ion.Molecular pharmacology · 2010Article
- Structural modeling of calcium binding in the selectivity filter of the L-type calcium channel.European biophysics journal : EBJ · 2010Article
- Docking of calcium ions in proteins with flexible side chains and deformable backbones.European biophysics journal : EBJ · 2010Article
- A homology model of the pore domain of a voltage-gated calcium channel is consistent with available SCAM data.The Journal of general physiology · 2010Article
- Docking flexible ligands in proteins with a solvent exposure- and distance-dependent dielectric function.Journal of computer-aided molecular design · 2010Article
- Use of Kv1.3 blockers for inflammatory skin conditions.Current medicinal chemistry · 2010Review
- Voltage-gated potassium channels as therapeutic targets.Nature reviews. Drug discovery · 2009Review
- Structural model for dihydropyridine binding to L-type calcium channels.The Journal of biological chemistry · 2009Article
- K+ channel modulators for the treatment of neurological disorders and autoimmune diseases.Chemical reviews · 2008Review
- Sodium channels: ionic model of slow inactivation and state-dependent drug binding.Biophysical journal · 2007Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCorreolide, a nortriterpene isolated from the Costa Rican tree Spachea correa, is a novel immunosuppressant, which blocks Kv1.3 channels in human T lymphocytes. Earlier mutational studies suggest that correolide binds in the channel pore. Correolide has several nucleophilic groups, but the pore-lining helices in Kv1.3 are predominantly hydrophobic raising questions about the nature of correolide-channel interactions.
resultsWe employed the method of Monte Carlo (MC) with energy minimization to search for optimal complexes of correolide in Kv1.2-based models of the open Kv1.3 with potassium binding sites 2/4 or 1/3/5 loaded with K+ ions. The energy was MC-minimized from many randomly generated starting positions and orientations of the ligand. In all the predicted low-energy complexes, oxygen atoms of correolide chelate a K+ ion. Correolide-sensing residues known from mutational analysis along with the ligand-bound K+ ion provide major contributions to the ligand-binding energy. Deficiency of K+ ions in the selectivity filter of C-type inactivated Kv1.3 would stabilize K+-bound correolide in the inner pore.
conclusionOur study explains the paradox that cationic and nucleophilic ligands bind to the same region in the inner pore of K+ channels and suggests that a K+ ion is an important determinant of the correolide receptor and possibly receptors of other nucleophilic blockers of the inner pore of K+ channels.
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