1yxq
From Proteopedia
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|PDB= 1yxq |SIZE=350|CAPTION= <scene name='initialview01'>1yxq</scene>, resolution 2.01Å | |PDB= 1yxq |SIZE=350|CAPTION= <scene name='initialview01'>1yxq</scene>, resolution 2.01Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SWI:SWINHOLIDE+A'>SWI</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yxq OCA], [http://www.ebi.ac.uk/pdbsum/1yxq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yxq RCSB]</span> | ||
}} | }} | ||
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[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: Tanaka, J.]] | [[Category: Tanaka, J.]] | ||
| - | [[Category: | + | [[Category: actin]] |
| - | [[Category: | + | [[Category: macrolide toxin]] |
| - | [[Category: | + | [[Category: swinholide some]] |
| - | + | ||
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:26:05 2008'' |
Revision as of 22:26, 30 March 2008
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| , resolution 2.01Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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