Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.

@article{Istvan2000CrystalSO,
  title={Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.},
  author={Eva S Istvan and Maya Palnitkar and Susan K Buchanan and Johann Deisenhofer},
  journal={The EMBO journal},
  year={2000},
  volume={19 5},
  pages={819-30}
}
3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the formation of mevalonate, the committed step in the biosynthesis of sterols and isoprenoids. The activity of HMGR is controlled through synthesis, degradation and phosphorylation to maintain the concentration of mevalonate-derived products. In addition to the physiological regulation of HMGR, the human enzyme has been targeted successfully by drugs in the clinical treatment of high serum cholesterol levels. Three crystal structures of… CONTINUE READING