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Título: | Zampanolide, a potent new microtubule stabilizing agent, covalently reacts with the taxane luminal site in both tubulin alpha-beta-heterodimers and microtubules |
Autor: | Field, Jessica J.; Pera, Benet CSIC; Calvo, Enrique; Canales, Ángeles CSIC ORCID; Zurwerra, Didier; Trigili, Chiara CSIC; Rodríguez-Salarichs, Javier CSIC; Matesanz, Ruth CSIC ; Kanakkanthara, Arun; Wakefield, St. John; Singh, A. Jonathan; Jiménez-Barbero, Jesús CSIC ORCID; Northcote, Peter; Miller, John H.; López, Juan Antonio; Hamel, Ernest; Barasoain, Isabel CSIC ; Altmann, Karl-Heinz; Díaz, José Fernando CSIC ORCID | Fecha de publicación: | 22-jun-2012 | Editor: | Elsevier | Citación: | Chemistry and Biology 19(6):686–698(2012) | Resumen: | Zampanolide and its less active analog dactylolide compete with paclitaxel for binding to microtubules and represent a new class of microtubule-stabilizing agent (MSA). Mass spectrometry demonstrated that the mechanism of action of both compounds involved covalent binding to β-tubulin at residues N228 and H229 in the taxane site of the microtubule. Alkylation of N228 and H229 was also detected in α,β-tubulin dimers. However, unlike cyclostreptin, the other known MSA that alkylates β-tubulin, zampanolide was a strong MSA. Modeling the structure of the adducts, using the NMR-derived dactylolide conformation, indicated that the stabilizing activity of zampanolide is likely due to interactions with the M-loop. Our results strongly support the existence of the luminal taxane site of microtubules in tubulin dimers and suggest that microtubule nucleation induction by MSAs may proceed through an allosteric mechanism | Descripción: | 13 páginas, 3 figuras, 1 tabla -- PAGS nros. 686-698 | Versión del editor: | http://dx.doi.org/10.1016/j.chembiol.2012.05.008 | URI: | http://hdl.handle.net/10261/60257 | DOI: | 10.1016/j.chembiol.2012.05.008 | ISSN: | 1074-5521 | E-ISSN: | 1879-1301 |
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