2fxu: Difference between revisions
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<StructureSection load='2fxu' size='340' side='right'caption='[[2fxu]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='2fxu' size='340' side='right'caption='[[2fxu]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fxu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2fxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxu OCA], [https://pdbe.org/2fxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxu RCSB], [https://www.ebi.ac.uk/pdbsum/2fxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Kossiakoff | [[Category: Kossiakoff AA]] | ||
[[Category: Kozmin | [[Category: Kozmin SA]] | ||
[[Category: Rizvi | [[Category: Rizvi SA]] | ||
[[Category: Tereshko | [[Category: Tereshko V]] | ||
Latest revision as of 12:33, 30 August 2023
X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
Structural highlights
FunctionACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedBistramide 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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