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| | <StructureSection load='5whf' size='340' side='right'caption='[[5whf]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='5whf' size='340' side='right'caption='[[5whf]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5whf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5whf]] is a 8 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=5WHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WHF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5whf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whf OCA], [http://pdbe.org/5whf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5whf RCSB], [http://www.ebi.ac.uk/pdbsum/5whf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5whf ProSAT]</span></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=5whf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whf OCA], [https://pdbe.org/5whf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5whf RCSB], [https://www.ebi.ac.uk/pdbsum/5whf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5whf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Obiero, J M]] | + | [[Category: Obiero JM]] |
| - | [[Category: Pang, A H]] | + | [[Category: Pang AH]] |
| - | [[Category: Tsodikov, O V]] | + | [[Category: Tsodikov OV]] |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Helical domain]]
| + | |
| - | [[Category: Intermediate filament]]
| + | |
| - | [[Category: Oligomerization]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
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.[1] Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.[2]
Publication Abstract from PubMed
Vimentin is an intermediate filament (IF) protein that is expressed in leukocytes, fibroblasts and endothelial cells of blood vessels. Vimentin filaments contribute to structural stability of the cell membrane, organelle positioning and protein transport. Vimentin self-assembles into a dimer that subsequently forms high-order structures, including tetramers and octamers. The details of IF assembly at crystallographic resolutions are limited to the tetrameric form. We describe a crystal structure of a fragment of a vimentin rod domain (coil 1B) with a dimer of tetramers in the asymmetric unit. Coil 1B in the crystal is in an infinitely high-order filamentous assembly state, in which the tetramers are packed against each other laterally in an antiparallel fashion across the crystal lattice. In one of the directions of lateral packing, the tetramers pack against each other strictly head-to-tail, and in the orthogonal direction the tetramers pack in a staggered manner. This organization of the tetramers of coil 1B in the crystal lattice, together with previously reported biochemical and structural data, yield a model of high-order vimentin filament assembly. DATABASE: Structural data are available in the PDB under the accession number 5WHF.
A crystal structure of coil 1B of vimentin in the filamentous form provides a model of a high-order assembly of a vimentin filament.,Pang AH, Obiero JM, Kulczyk AW, Sviripa VM, Tsodikov OV FEBS J. 2018 Jun 15. doi: 10.1111/febs.14585. PMID:29905014[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Challa AA, Stefanovic B. A novel role of vimentin filaments: binding and stabilization of collagen mRNAs. Mol Cell Biol. 2011 Sep;31(18):3773-89. doi: 10.1128/MCB.05263-11. Epub 2011 Jul , 11. PMID:21746880 doi:10.1128/MCB.05263-11
- ↑ Challa AA, Stefanovic B. A novel role of vimentin filaments: binding and stabilization of collagen mRNAs. Mol Cell Biol. 2011 Sep;31(18):3773-89. doi: 10.1128/MCB.05263-11. Epub 2011 Jul , 11. PMID:21746880 doi:10.1128/MCB.05263-11
- ↑ Pang AH, Obiero JM, Kulczyk AW, Sviripa VM, Tsodikov OV. A crystal structure of coil 1B of vimentin in the filamentous form provides a model of a high-order assembly of a vimentin filament. FEBS J. 2018 Jun 15. doi: 10.1111/febs.14585. PMID:29905014 doi:http://dx.doi.org/10.1111/febs.14585
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