V体育ios版 - Structural basis of swinholide A binding to actin
- PMID: 15797212
- DOI: 10.1016/j.chembiol.2005.02.011 (VSports注册入口)
"V体育官网" Structural basis of swinholide A binding to actin
Abstract
Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds VSports手机版. Here we present a 2. 0 A 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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