1YXQ
Crystal structure of actin in complex with swinholide A
Summary for 1YXQ
| Entry DOI | 10.2210/pdb1yxq/pdb |
| Descriptor | actin, alpha skeletal muscle, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | actin; swinholide a; macrolide toxin, contractile protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm, cytoskeleton: P68135 |
| Total number of polymer chains | 2 |
| Total formula weight | 86352.55 |
| Authors | Klenchin, V.A.,King, R.,Tanaka, J.,Marriott, G.,Rayment, I. (deposition date: 2005-02-22, release date: 2005-05-17, Last modification date: 2025-03-26) |
| Primary citation | Klenchin, V.A.,King, R.,Tanaka, J.,Marriott, G.,Rayment, I. Structural basis of swinholide a binding to actin Chem.Biol., 12:287-291, 2005 Cited by PubMed Abstract: Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. 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. PubMed: 15797212DOI: 10.1016/j.chembiol.2005.02.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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