2pav
From Proteopedia
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- | [[Image:2pav.png|left|200px]] | ||
- | < | + | ==Ternary complex of Profilin-Actin with the Last Poly-Pro of Human VASP== |
- | + | <StructureSection load='2pav' size='340' side='right'caption='[[2pav]], [[Resolution|resolution]] 1.80Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2pav]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PAV FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=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'>[https://proteopedia.org/fgij/fg.htm?mol=2pav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pav OCA], [https://pdbe.org/2pav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pav RCSB], [https://www.ebi.ac.uk/pdbsum/2pav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pav ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == 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. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pa/2pav_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pav ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin-actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin-actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin. | ||
- | + | Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.,Ferron F, Rebowski G, Lee SH, Dominguez R EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. PMID:17914456<ref>PMID:17914456</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2pav" style="background-color:#fffaf0;"></div> | |
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- | == | + | |
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==See Also== | ==See Also== | ||
- | *[[Actin]] | + | *[[Actin 3D structures|Actin 3D structures]] |
- | + | *[[Profilin 3D Structures|Profilin 3D Structures]] | |
- | == | + | *[[Vasodilator-stimulated phosphoprotein|Vasodilator-stimulated phosphoprotein]] |
- | < | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
- | [[Category: Dominguez | + | [[Category: Dominguez R]] |
- | [[Category: Ferron | + | [[Category: Ferron F]] |
- | [[Category: Rebowski | + | [[Category: Rebowski G]] |
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Current revision
Ternary complex of Profilin-Actin with the Last Poly-Pro of Human VASP
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