Publication | Open Access
The Absolute Configuration of Rhizopodin and Its Inhibition of Actin Polymerization by Dimerization
64
Citations
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References
2008
Year
Protein AssemblyMolecular BiologyCytoskeletonC2-symmetric BislactoneActin PolymerizationChemical BiologyProtein FoldingProtein X-ray CrystallographyBiophysicsAbsolute ConfigurationMacromolecular MachineBiomolecular InteractionMolecular MicrobiologyMacromolecular ArchitectureStructural BiologyActive ConformationNatural SciencesMacromolecular SystemCell MotilityMicrobiologyMedicineRhizopodin-induced Actin Dimerization
Three's company: Rhizopodin is a cytostatic macrolide and a potent actin depolymerizer produced by the myxobacterium Myxococcus stipitatus. A crystal structure analysis of the rhizopodin/actin complex reveals that rhizopodin is a C2-symmetric bislactone (see formula). The ternary complex supports the mode of rhizopodin-induced actin dimerization and reveals the absolute configuration and biologically active conformation of this macrolide.
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