2fxu
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(New page: 200px<br /><applet load="2fxu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fxu, resolution 1.35Å" /> '''X-ray Structure of B...)
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Revision as of 08:42, 21 November 2007
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X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
Overview
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 Å. 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 Structure
2FXU is a Single protein structure of sequence from Oryctolagus cuniculus with CA, ATP and BID as ligands. Full crystallographic information is available from OCA.
Reference
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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