Journal
CHEMISTRY & BIOLOGY
Volume 12, Issue 3, Pages 287-291Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2005.02.011
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Funding
- NIAMS NIH HHS [AR35186] Funding Source: Medline
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Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. Here we present a 2.0 angstrom resolution structure of swinholide A, a marine macrolide, bound to two actin molecules. The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other. The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization. The observed structure reveals the mechanism of action of swinholide A and provides a structural framework about which to design new agents directed at the cytoskeleton.
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