8rve: Difference between revisions
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==Vimentin intermediate filament== | |||
<StructureSection load='8rve' size='340' side='right'caption='[[8rve]], [[Resolution|resolution]] 7.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8rve]] is a 78 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RVE 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]] 7.2Å</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=8rve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rve OCA], [https://pdbe.org/8rve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rve RCSB], [https://www.ebi.ac.uk/pdbsum/8rve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rve ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VIME_HUMAN VIME_HUMAN] Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.<ref>PMID:21746880</ref> Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.<ref>PMID:21746880</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Intermediate filaments (IFs) are integral components of the cytoskeleton. They provide cells with tissue-specific mechanical properties and are involved in numerous cellular processes. Due to their intricate architecture, a 3D structure of IFs has remained elusive. Here we use cryo-focused ion-beam milling, cryo-electron microscopy and tomography to obtain a 3D structure of vimentin IFs (VIFs). VIFs assemble into a modular, intertwined and flexible helical structure of 40 alpha-helices in cross-section, organized into five protofibrils. Surprisingly, the intrinsically disordered head domains form a fiber in the lumen of VIFs, while the intrinsically disordered tails form lateral connections between the protofibrils. Our findings demonstrate how protein domains of low sequence complexity can complement well-folded protein domains to construct a biopolymer with striking mechanical strength and stretchability. | |||
Vimentin filaments integrate low-complexity domains in a complex helical structure.,Eibauer M, Weber MS, Kronenberg-Tenga R, Beales CT, Boujemaa-Paterski R, Turgay Y, Sivagurunathan S, Kraxner J, Koster S, Goldman RD, Medalia O Nat Struct Mol Biol. 2024 Jun;31(6):939-949. doi: 10.1038/s41594-024-01261-2. , Epub 2024 Apr 17. PMID:38632361<ref>PMID:38632361</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8rve" style="background-color:#fffaf0;"></div> | ||
[[Category: Eibauer | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Eibauer M]] | |||
[[Category: Medalia O]] | |||
