Research Topics
Species | E S IstvanSummaryAffiliation: Washington University School of Medicine Country: USA Publications
| Collaborators |
Detail Information
Publications
Structural mechanism for statin inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductaseEva S Istvan
Howard Hughes Medical Institute and Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA
Am Heart J 144:S27-32. 2002..The flexibility of these residues is critical for binding with statins; if ordered, they would sterically hinder such binding...
Statin inhibition of HMG-CoA reductase: a 3-dimensional viewEva Istvan
Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, Campus Box 8230, 660 South Euclid Avenue, St Louis, MO 63110, USA
Atheroscler Suppl 4:3-8. 2003..Differences in statin structure and binding characteristics may partially contribute to differences in potency of HMG-CoA reductase inhibition and other pharmacologic properties...
Bacterial and mammalian HMG-CoA reductases: related enzymes with distinct architecturesE S Istvan
Howard Hughes Medical Institute and Department of Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA
Curr Opin Struct Biol 11:746-51. 2001..An appreciation of the remarkable differences in the active site architecture may ultimately lead to the development of novel antibacterial agents...
Structural mechanism for statin inhibition of HMG-CoA reductaseE S Istvan
Department of Biochemistry, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, TX 75390 9050, USA
Science 292:1160-4. 2001..Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding...
Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysisE S Istvan
Howard Hughes Medical Institute, Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, TX 75235 9050, USA
EMBO J 19:819-30. 2000..The active site architecture of human HMGR is different from that of bacterial HMGR; this may explain why binding of HMGR inhibitors to bacterial HMGRs has not been reported...
