1yxq
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1yxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxq, resolution 2.01Å" /> '''Crystal structure of...)
Next diff →
Revision as of 05:00, 21 November 2007
|
Crystal structure of actin in complex with swinholide A
Overview
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.
About this Structure
1YXQ is a Single protein structure of sequence from Oryctolagus cuniculus with MG, ATP, SWI and EDO as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of swinholide A binding to actin., Klenchin VA, King R, Tanaka J, Marriott G, Rayment I, Chem Biol. 2005 Mar;12(3):287-91. PMID:15797212
Page seeded by OCA on Wed Nov 21 07:07:21 2007
