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| {{STRUCTURE_1gk7| PDB=1gk7 | SCENE= }} | | {{STRUCTURE_1gk7| PDB=1gk7 | SCENE= }} |
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| '''HUMAN VIMENTIN COIL 1A FRAGMENT (1A)'''
| | ===HUMAN VIMENTIN COIL 1A FRAGMENT (1A)=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11889032}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11889032 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11889032}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Intermediate filament]] | | [[Category: Intermediate filament]] |
| [[Category: Vimentin]] | | [[Category: Vimentin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:40:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:25:31 2008'' |
