View source for 3trt


==Crystal structure of stabilised vimentin coil2 fragment==
<StructureSection load='3trt' size='340' side='right'caption='[[3trt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3trt]] is a 2 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3trt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chernyatina AA]]
[[Category: Strelkov SV]]