Toward docking-based virtual screening for discovering antitubulin agents by targeting taxane and colchicine binding sites.
Tubulin proteins play a major role in cell division, and were first identified as attractive targets for cancer therapy over 40 years ago. Recent studies aiming to gain structural insight into the binding mode of antitubulin agents to taxane or colchicine binding sites using NMR and/or molecular-mechanics-assisted conformation analysis and docking simulations have been reported. These studies, which represent the main focus of this article, create prospects for the development of docking-based virtual screening techniques to aid in the discovery of new antitubulin agents.
Soulère
Laurent
L
Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Villeurbanne, France. laurent.soulere@insa-lyon.fr
D001665:Binding Sites; D003078:Colchicine / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D043823:Taxoids / Q000737:chemistry*; D014404:Tubulin / Q000737:chemistry / Q000187:drug effects*
D043823:Taxoids; D014404:Tubulin; D003078:Colchicine