Maytansine inhibits nucleotide binding at the exchangeable site of tubulin

作者: Abbott B. Huang , Chii M. Lin , Ernest Hamel

DOI: 10.1016/0006-291X(85)91073-3

关键词:

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

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