Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B.
This paper summarizes published data on the interactions of tubulin with antimitotic compounds that inhibit the binding of vinca alkaloids to the protein. These are all relatively complex natural products isolated from higher plants, fungi and marine invertebrate animals. These agents are maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B and their congeners. Effects on tubulin polymerization, ligand binding interactions and structure-activity relationships are emphasized.
Hamel
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Laboratory of Molecular Pharmacology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
D000818:Animals; D000903:Antibiotics, Antineoplastic / Q000494:pharmacology; D000970:Antineoplastic Agents / Q000494:pharmacology*; D047630:Depsipeptides; D004988:Ethers, Cyclic / Q000494:pharmacology; D007783:Lactones / Q000494:pharmacology; D018942:Macrolides; D008453:Maytansine / Q000494:pharmacology; D009183:Mycotoxins / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology; D014404:Tubulin / Q000187:drug effects* / Q000378:metabolism; D014748:Vinca Alkaloids / Q000378:metabolism / Q000494:pharmacology*; D000095662:Polyether Polyketides
D000903:Antibiotics, Antineoplastic; D000970:Antineoplastic Agents; D047630:Depsipeptides; D004988:Ethers, Cyclic; D007783:Lactones; D018942:Macrolides; D008453:Maytansine; D009183:Mycotoxins; D009842:Oligopeptides; D014404:Tubulin; D014748:Vinca Alkaloids; C075610:dolastatin 15; C070519:halichondrin B; D000095662:Polyether Polyketides; C035753:phomopsin; C041443:rhizoxin; C064570:dolastatin 10