title: Computational study of binding of epothilone A to β-tubulin.
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.
authors.affiliation: Laboratory of Theory of Biopolymers, Faculty of Chemistry, University of Warsaw, Warszawa, Poland.
authors.forename: Karol
authors.initials: K
authors.lastname: Kamel
authors.forename: Andrzej
authors.initials: A
authors.lastname: Kolinski
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003198:Computer Simulation; D034261:Epothilones / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011485:Protein Binding; D013816:Thermodynamics; D014404:Tubulin / Q000737:chemistry*
chemical_list: D034261:Epothilones; D014404:Tubulin; C093787:epothilone A