Journal of Biotechnology & Biomaterials
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Coronary artery disease isone of the most investigated diseases in medicinal chemistry. HMG-CoA reductase (or 3-hydroxy-
3-methyl-glutaryl-CoA reductase or HMGCR) is the rate-controlling enzyme of the mevalonate pathway, the metabolic
pathway that produces cholesterol and other isoprenoids. Normally in mammalian cells this enzyme is suppressed by cholesterol
derived from the internalization and degradation of low density lipoprotein (LDL) via the LDL receptor as well as oxidized species
of cholesterol. This enzyme is thus the target of the widely available cholesterol-lowering drugs known collectively as the statins.
In present study crystal structure of HMG-coA 1HWK was prepared. Active site was identified. Virtual screening was
performed against ligand data set prepared from different literature search and ZINC data base to identify a lead molecule. This
lead molecule was optimized using molecular dynamics. These lead molecules show good docking score than statins.
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