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1gk4
From Proteopedia
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|PDB= 1gk4 |SIZE=350|CAPTION= <scene name='initialview01'>1gk4</scene>, resolution 2.30Å | |PDB= 1gk4 |SIZE=350|CAPTION= <scene name='initialview01'>1gk4</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=STA:Coiled-Coil+Stutter'>STA</scene> | |SITE= <scene name='pdbsite=STA:Coiled-Coil+Stutter'>STA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1gk4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gk4 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Inflammatory response, modulation of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607918 607918]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Strelkov, S V.]] | [[Category: Strelkov, S V.]] | ||
[[Category: Zimbelmann, R.]] | [[Category: Zimbelmann, R.]] | ||
| - | [[Category: ACT]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: heptad repeat]] | [[Category: heptad repeat]] | ||
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[[Category: stutter]] | [[Category: stutter]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:45:43 2008'' |
Revision as of 17:45, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN VIMENTIN COIL 2B FRAGMENT (CYS2)
Overview
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.
About this Structure
1GK4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 20:45:43 2008
