Abstract
Structure-based virtual screening identified pyrimidine-2,4,6-trione and 4H-1,2,4-triazole-3-thiol as novel scaffolds of Hsp90 ATPase inhibitors. Their binding modes in the ATP-binding pocket of Hsp90 were analyzed using AutoDoc program combined with molecular dynamics (MD) simulations.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Antineoplastic Agents / chemistry*
-
Antineoplastic Agents / pharmacology
-
Binding Sites
-
Cell Line, Tumor
-
Combinatorial Chemistry Techniques
-
Computer Simulation
-
Databases, Factual
-
HSP90 Heat-Shock Proteins / antagonists & inhibitors*
-
HSP90 Heat-Shock Proteins / metabolism
-
Humans
-
Pyrimidines / chemistry*
-
Receptor, ErbB-2 / metabolism
-
Triazoles / chemistry*
Substances
-
Antineoplastic Agents
-
HSP90 Heat-Shock Proteins
-
Pyrimidines
-
Triazoles
-
1,2,4-triazole
-
Receptor, ErbB-2