%0 Journal Article %J Acta Biochimica Polonica %D 2011 %T Computational study of binding of epothilone A to β-tubulin %A Karol Kamel %A Andrzej Koliński %K Animals %K Binding Sites %K Cattle %K Computer Simulation %K Epothilones %K Epothilones: chemistry %K Hydrogen Bonding %K Models %K Molecular %K Protein Binding %K Thermodynamics %K Tubulin %K Tubulin: chemistry %X 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. %B Acta Biochimica Polonica %V 58 %P 255–60 %8 jan %G eng %U http://www.ncbi.nlm.nih.gov/pubmed/21633729