1yxq: Difference between revisions

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[[Image:1yxq.gif|left|200px]]
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{{STRUCTURE_1yxq|  PDB=1yxq  |  SCENE=  }}  
{{STRUCTURE_1yxq|  PDB=1yxq  |  SCENE=  }}  


'''Crystal structure of actin in complex with swinholide A'''
===Crystal structure of actin in complex with swinholide A===




==Overview==
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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 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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{{ABSTRACT_PUBMED_15797212}}


==About this Structure==
==About this Structure==
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[[Category: Macrolide toxin]]
[[Category: Macrolide toxin]]
[[Category: Swinholide some]]
[[Category: Swinholide some]]
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Revision as of 23:35, 28 July 2008

File:1yxq.png

Template:STRUCTURE 1yxq

Crystal structure of actin in complex with swinholide ACrystal structure of actin in complex with swinholide A

Template:ABSTRACT PUBMED 15797212

About this StructureAbout this Structure

1YXQ is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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