Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites.
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منابع مشابه
Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites.
Dolastatin 10, a potent antimitotic peptide from a marine animal, strongly inhibits microtubule assembly, tubulin-dependent GTP hydrolysis, and the binding of vinca alkaloids to tubulin. In studies of the binding of [3H]vincristine to the protein, with vinblastine as a control for competitive inhibition (Ki, 6.6 microM), we found that the macrolide antimitotic agents maytansine and rhizoxin wer...
متن کاملMolecular Modeling Studies on Vinblastine Binding Site of Tubulin for Antimitotic agents
Medicinal chemistry depends on many other disciplines ranging from organic chemistry andpharmacology to computational chemistry. Typically medicinal chemists use the moststraightforward ways to prepare compounds. The validation of any design project comes from thebiological testing.Studies of the binding site of vinblastine by a single cross—linking experiment identified it asbeing between resi...
متن کاملmolecular modeling studies on vinblastine binding site of tubulin for antimitotic agents
medicinal chemistry depends on many other disciplines ranging from organic chemistry andpharmacology to computational chemistry. typically medicinal chemists use the moststraightforward ways to prepare compounds. the validation of any design project comes from thebiological testing.studies of the binding site of vinblastine by a single cross—linking experiment identified it asbeing between resi...
متن کاملBinding of fluorescent analogs of GTP to the exchangeable nucleotide binding site of tubulin.
6 S tubulin from which the exchangeably bound guanine nucleotide had been removed was examined for its ability to bind two fluorescent analogs of GTP. One analog, (y-AmNS)GTP, contains the fluorophore l-aminonaphthalene 5-sulfonate attached to the y phosphate of GTP via a phosphoamidate bond. The second analog contains the same fluorophore attached to the sulfur atom of GTP-y-S via a 5-atom lin...
متن کاملTubulin-based structure-affinity relationships for antimitotic Vinca alkaloids.
The Vinca alkaloids are a group of widely used anticancer drugs, originally extracted from the Madagascar periwinkle, that disrupt microtubule dynamics in mammalian cells by interfering with proper assembly of α,β-tubulin heterodimers. They favor curved tubulin assemblies that destabilize microtubules and induce formation of spiral aggregates. Their binding energy profiles have been characteriz...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44880-0