2fxu: Difference between revisions
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|PDB= 2fxu |SIZE=350|CAPTION= <scene name='initialview01'>2fxu</scene>, resolution 1.35Å | |PDB= 2fxu |SIZE=350|CAPTION= <scene name='initialview01'>2fxu</scene>, resolution 1.35Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BID:BISTRAMIDE+A'>BID</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxu OCA], [http://www.ebi.ac.uk/pdbsum/2fxu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fxu RCSB]</span> | |||
}} | }} | ||
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[[Category: Rizvi, S A.]] | [[Category: Rizvi, S A.]] | ||
[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
[[Category: actin complexed to bistramide some]] | [[Category: actin complexed to bistramide 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 03:09:07 2008'' | ||
Revision as of 03:09, 31 March 2008
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| , resolution 1.35Å | |||||||
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
OverviewOverview
Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric actin at a resolution of 1.35 A. The most notable aspect of the bistramide A-actin structure is an extensive hydrogen-bonding network established upon a deep penetration of the central segment of bistramide A into the actin-binding cleft between subdomains 1 and 3. The structure presents the first insight into the observed ability of bistramide A to modulate G-actin polymerization. The structural information combined with our ability to chemically modify the bistramide framework provides the basis for rational development of a series of new synthetic analogues as useful probes for studying actin cytoskeleton and as potential therapeutic leads.
About this StructureAbout this Structure
2FXU is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of bistramide A-actin complex at a 1.35 angstroms resolution., Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA, J Am Chem Soc. 2006 Mar 29;128(12):3882-3. PMID:16551075
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