1yxq: Difference between revisions
New page: left|200px<br /><applet load="1yxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxq, resolution 2.01Å" /> '''Crystal structure of... |
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[[Image:1yxq.gif|left|200px]]<br /><applet load="1yxq" size=" | [[Image:1yxq.gif|left|200px]]<br /><applet load="1yxq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1yxq, resolution 2.01Å" /> | caption="1yxq, resolution 2.01Å" /> | ||
'''Crystal structure of actin in complex with swinholide A'''<br /> | '''Crystal structure of actin in complex with swinholide A'''<br /> | ||
==Overview== | ==Overview== | ||
Marine toxins targeting the actin cytoskeleton represent a new and | 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== | ==About this Structure== | ||
1YXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG, ATP, SWI and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1YXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene>, <scene name='pdbligand=SWI:'>SWI</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: King, R.]] | [[Category: King, R.]] | ||
[[Category: Klenchin, V | [[Category: Klenchin, V A.]] | ||
[[Category: Marriott, G.]] | [[Category: Marriott, G.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
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[[Category: actin; swinholide a; macrolide toxin]] | [[Category: actin; swinholide a; macrolide toxin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:10 2008'' | ||
Revision as of 17:10, 21 February 2008
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Crystal structure of actin in complex with swinholide A
OverviewOverview
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 StructureAbout this Structure
1YXQ is a Single protein structure of sequence from Oryctolagus cuniculus with , , and as ligands. 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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