This week in techniques



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Crystal structure of ab-tubulin in complex with anticancer microtubule-stabilizing agents

Protein crystal structure studies identified the molecular mechanism of microtubule-stabilizing cancer therapeutics, which could help guide the development of new treatments. Crystallography studies of ab-tubulin complexed with two microtubule-stabilizing cancer therapies-zampanolide and epothilone A-showed that the compounds bind to a hydrophobic pocket on the tubulin-b subunit known as the taxane pocket. Next steps include using the structural data to develop analogs of zampanolide and epothilone A and investigating the mechanism of additional tubulin-targeting compounds.
Zampanolide and epothilone A are research reagents.

SciBX 6(3); doi:10.1038/scibx.2013.72
Published online Jan. 24, 2013

Unpatented; licensing status not applicable

Prota, A.E. et al. Science; published online Jan. 3, 2013;
Contact: Michel O. Steinmetz, Paul Scherrer Institute, Villigen, Switzerland