How Reliable Are Current Docking Approaches for Structure-Based Drug Design? Lessons from Aldose Reductase
Two related inhibitors were flexibly docked into different conformers of aldose reductase. Although the overall binding topologies were roughly matched, significant deviations are observed in the subsequently determined crystal structures. Flexible redocking into the crystallographically observed pr...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2007-01, Vol.46 (19), p.3575-3578 |
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| container_end_page | 3578 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Zentgraf, Matthias Steuber, Holger Koch, Cornelia La Motta, Concettina Sartini, Stefania Sotriffer, Christoph A. Klebe, Gerhard |
| description | Two related inhibitors were flexibly docked into different conformers of aldose reductase. Although the overall binding topologies were roughly matched, significant deviations are observed in the subsequently determined crystal structures. Flexible redocking into the crystallographically observed protein conformers achieves, however, perfect binding‐position predictions. |
| doi_str_mv | 10.1002/anie.200603625 |
| format | Article |
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| identifier | ISSN: 1433-7851 |
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| subjects | Aldehyde Reductase - antagonists & inhibitors Aldehyde Reductase - metabolism aldose reductase Binding Sites Computer Simulation crystal structure analysis Crystallography, X-Ray Databases, Factual docking methods Drug Design Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - pharmacology Ligands protein-ligand complexes Structure-Activity Relationship |
| title | How Reliable Are Current Docking Approaches for Structure-Based Drug Design? Lessons from Aldose Reductase |
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