1yxq: Difference between revisions
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==Crystal structure of actin in complex with swinholide A== | ==Crystal structure of actin in complex with swinholide A== | ||
<StructureSection load='1yxq' size='340' side='right' caption='[[1yxq]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='1yxq' size='340' side='right'caption='[[1yxq]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yxq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YXQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yxq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YXQ FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1yxq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1yxq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Actin 3D structures|Actin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: European rabbit]] | [[Category: European rabbit]] | ||
[[Category: Large Structures]] | |||
[[Category: King, R]] | [[Category: King, R]] | ||
[[Category: Klenchin, V A]] | [[Category: Klenchin, V A]] | ||
Revision as of 12:23, 24 July 2019
Crystal structure of actin in complex with swinholide ACrystal structure of actin in complex with swinholide A
Structural highlights
Function[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedMarine 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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