Molecular docking of the highly hypolipidemic agent alpha-asarone with the catalytic portion of HMG-CoA reductase.
Article Details
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Medina-Franco JL, Lopez-Vallejo F, Rodriguez-Morales S, Castillo R, Chamorro G, Tamariz J
Molecular docking of the highly hypolipidemic agent alpha-asarone with the catalytic portion of HMG-CoA reductase.
Bioorg Med Chem Lett. 2005 Feb 15;15(4):989-94.
- PubMed ID
- 15686898 [ View in PubMed]
- Abstract
Docking experiments using a number of published crystal structures of HMG-CoA reductase with the potent hypocholesterolemic agent alpha-asarone are described. The results indicate that alpha-asarone binds in the enzyme's active site. The methoxy groups play a key role in the binding and probably also in its biological activity, as shown by extensive SAR studies reported for analogues of alpha-asarone. The docking results will be valuable for the structure-based design of novel hypolipidemic agents.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Meglutol 3-hydroxy-3-methylglutaryl-coenzyme A reductase IC 50 (nM) 4000 N/A N/A Details Meglutol 3-hydroxy-3-methylglutaryl-coenzyme A reductase Ki (nM) 23.5 N/A N/A Details Rosuvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase IC 50 (nM) 5.4 N/A N/A Details Rosuvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase Ki (nM) 0.9 N/A N/A Details Rosuvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase Ki (nM) 71000 N/A N/A Details Simvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase Ki (nM) 68000 N/A N/A Details Simvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase Ki (nM) 2.6 N/A N/A Details Simvastatin 3-hydroxy-3-methylglutaryl-coenzyme A reductase IC 50 (nM) 11.2 N/A N/A Details