2fxu: Difference between revisions
New page: left|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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[[Image:2fxu.gif|left|200px]]<br /><applet load="2fxu" size=" | [[Image:2fxu.gif|left|200px]]<br /><applet load="2fxu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fxu, resolution 1.35Å" /> | caption="2fxu, resolution 1.35Å" /> | ||
'''X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.'''<br /> | '''X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.'''<br /> | ||
==Overview== | ==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 | 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 Structure== | ==About this Structure== | ||
2FXU 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 CA, ATP and BID as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2FXU 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=CA:'>CA</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=BID:'>BID</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kossiakoff, A | [[Category: Kossiakoff, A A.]] | ||
[[Category: Kozmin, S | [[Category: Kozmin, S A.]] | ||
[[Category: Rizvi, S | [[Category: Rizvi, S A.]] | ||
[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: actin complexed to bistramide a]] | [[Category: actin complexed to bistramide a]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:12 2008'' | ||
Revision as of 18:26, 21 February 2008
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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 with , and as ligands. 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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