@article {Kamel2011, title = {Computational study of binding of epothilone A to β-tubulin}, journal = {Acta Biochimica Polonica}, volume = {58}, number = {2}, year = {2011}, month = {jan}, pages = {255{\textendash}60}, abstract = {Understanding the interactions of epothilones with β-tubulin is crucial for computer aided rational design of macrocyclic drugs based on epothilones and epothilone derivatives. Despite numerous structure-activity relationship investigations we still lack substantial knowledge about the binding mode of epothilones and their derivatives to β-tubulin. In this work, we reevaluated the electron crystallography structure of epothilone A/β-tubulin complex (PDB entry 1TVK) and proposed an alternative binding mode of epothilone A to β-tubulin that explains more experimental facts.}, keywords = {Animals, Binding Sites, Cattle, Computer Simulation, Epothilones, Epothilones: chemistry, Hydrogen Bonding, Models, Molecular, Protein Binding, Thermodynamics, Tubulin, Tubulin: chemistry}, issn = {1734-154X}, url = {http://www.ncbi.nlm.nih.gov/pubmed/21633729}, author = {Karol Kamel and Andrzej Koli{\'n}ski} }