8vkh
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of gelsolin domains G1-G3 bound to the barbed end of F-actin== | |
| + | <StructureSection load='8vkh' size='340' side='right'caption='[[8vkh]], [[Resolution|resolution]] 3.63Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8vkh]] is a 8 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=8VKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VKH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.63Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <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=8vkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vkh OCA], [https://pdbe.org/8vkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vkh RCSB], [https://www.ebi.ac.uk/pdbsum/8vkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vkh 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gelsolin is the prototypical member of a family of Ca (2+) -dependent F-actin severing and capping proteins. A structure of Ca (2+) -bound full-length gelsolin at the barbed end shows domains G1G6 and the inter-domain linkers wrapping around F-actin. Another structure shows domains G1G3, a fragment produced during apoptosis, on both sides of F-actin. Conformational changes that trigger severing occur on one side of F-actin with G1G6 and on both sides with G1G3. Gelsolin remains bound after severing, blocking subunit exchange. | ||
| - | + | Mechanism of Actin Filament Severing and Capping by Gelsolin.,Barrie KR, Rebowski G, Dominguez R bioRxiv [Preprint]. 2024 Sep 23:2024.09.10.612341. doi: , 10.1101/2024.09.10.612341. PMID:39345426<ref>PMID:39345426</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8vkh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Barrie KR]] | ||
| + | [[Category: Dominguez R]] | ||
| + | [[Category: Rebowski G]] | ||
Current revision
Structure of gelsolin domains G1-G3 bound to the barbed end of F-actin
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