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3trt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3trt is ON HOLD Authors: Chernyatina, A.A., Strelkov, S.V. Description: Crystal structure of stabilised vimentin coil2 fragment) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of stabilised vimentin coil2 fragment== | |
| + | <StructureSection load='3trt' size='340' side='right'caption='[[3trt]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3trt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TRT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3klt|3klt]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3trt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trt OCA], [https://pdbe.org/3trt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3trt RCSB], [https://www.ebi.ac.uk/pdbsum/3trt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3trt 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 == | ||
| + | Cytoskeletal intermediate filaments (IFs) assemble from the elementary dimers based on a segmented alpha-helical coiled-coil (CC) structure. Crystallographic studies of IF protein fragments remain the main route to access their atomic structure. To enable crystallization, such fragments must be sufficiently short. As a consequence, they often fail to assemble into the correct CC dimers. In particular, human vimentin fragment D3 corresponding to the first half of coil2 (residues 261-335) stays monomeric in solution. We have induced its dimerization via introducing a disulfide link between two cysteines engineered in the hydrophobic core of the CC close to its N-terminus. The 2.3A crystal structure of the D3st (stabilized) fragment reveals a mostly parallel alpha-helical bundle structure in its N-terminal half which smoothly continues into a left-handed CC towards the C-terminus. This provides a direct evidence for a continuously alpha-helical structure of the coil2 segment and disproves the previously suggested existence of linker L2 separating it into two left-handed CCs. The general principles of CC dimer stabilization by disulfide introduction are also discussed. | ||
| - | + | Stabilization of vimentin coil2 fragment via an engineered disulfide.,Chernyatina AA, Strelkov SV J Struct Biol. 2012 Jan;177(1):46-53. Epub 2011 Nov 18. PMID:22119849<ref>PMID:22119849</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3trt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chernyatina, A A]] | ||
| + | [[Category: Strelkov, S V]] | ||
| + | [[Category: Alpha-helix]] | ||
| + | [[Category: Cytoskeleton]] | ||
| + | [[Category: Intermediate filament]] | ||
| + | [[Category: Structural protein]] | ||
| + | [[Category: Vimentin]] | ||
Current revision
Crystal structure of stabilised vimentin coil2 fragment
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