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Biochem Biophys Res Commun. 1985 May 16;128(3):1239-46.

Maytansine inhibits nucleotide binding at the exchangeable site of tubulin.

Abstract

The antineoplastic drug maytansine inhibits the binding of exogenously added radiolabeled GDP and GTP to tubulin (50% inhibition at 9-10 microM drug at 0 degrees). Vinblastine was 1/10-th as inhibitory. Neither maytansine nor vinblastine displaced GDP from tubulin, and both drugs virtually eliminated dissociation of radiolabeled GDP from the exchangeable site. Maytansine also inhibits binding of nucleotides to a vacant exchangeable site. Maytansine thus prevents nucleotide exit and entry at the exchangeable site because of a direct physical obstruction or a conformational change in the tubulin molecule.

PMID:
4004859
DOI:
10.1016/0006-291x(85)91073-3
[Indexed for MEDLINE]

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