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| | <StructureSection load='1gk4' size='340' side='right'caption='[[1gk4]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1gk4' size='340' side='right'caption='[[1gk4]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gk4]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GK4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gk4]] is a 6 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=1GK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GK4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gk6|1gk6]], [[1gk7|1gk7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=1gk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk4 OCA], [http://pdbe.org/1gk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gk4 RCSB], [http://www.ebi.ac.uk/pdbsum/1gk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk4 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=1gk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk4 OCA], [https://pdbe.org/1gk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1gk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk4 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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aebi, U]] | + | [[Category: Aebi U]] |
| - | [[Category: Burkhard, P]] | + | [[Category: Burkhard P]] |
| - | [[Category: Geisler, N]] | + | [[Category: Geisler N]] |
| - | [[Category: Herrmann, H]] | + | [[Category: Herrmann H]] |
| - | [[Category: Strelkov, S V]] | + | [[Category: Strelkov SV]] |
| - | [[Category: Zimbelmann, R]] | + | [[Category: Zimbelmann R]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Heptad repeat]]
| + | |
| - | [[Category: Intermediate filament]]
| + | |
| - | [[Category: Parallel coiled coil]]
| + | |
| - | [[Category: Stutter]]
| + | |
| - | [[Category: Vimentin]]
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| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Intermediate filaments (IFs) are key components of the cytoskeleton in higher eukaryotic cells. The elementary IF 'building block' is an elongated coiled-coil dimer consisting of four consecutive alpha-helical segments. The segments 1A and 2B include highly conserved sequences and are critically involved in IF assembly. Based on the crystal structures of three human vimentin fragments at 1.4-2.3 A resolution (PDB entries 1gk4, 1gk6 and 1gk7), we have established the molecular organization of these two segments. The fragment corresponding to segment 1A forms a single, amphipatic alpha-helix, which is compatible with a coiled-coil geometry. While this segment might yield a coiled coil within an isolated dimer, monomeric 1A helices are likely to play a role in specific dimer-dimer interactions during IF assembly. The 2B segment reveals a double-stranded coiled coil, which unwinds near residue Phe351 to accommodate a 'stutter'. A fragment containing the last seven heptads of 2B interferes heavily with IF assembly and also transforms mature vimentin filaments into a new kind of structure. These results provide the first insight into the architecture and functioning of IFs at the atomic level.
Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly.,Strelkov SV, Herrmann H, Geisler N, Wedig T, Zimbelmann R, Aebi U, Burkhard P EMBO J. 2002 Mar 15;21(6):1255-66. PMID:11889032[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
- ↑ Strelkov SV, Herrmann H, Geisler N, Wedig T, Zimbelmann R, Aebi U, Burkhard P. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 2002 Mar 15;21(6):1255-66. PMID:11889032 doi:http://dx.doi.org/10.1093/emboj/21.6.1255
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