1gk7
From Proteopedia
(New page: 200px<br /> <applet load="1gk7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gk7, resolution 1.40Å" /> '''HUMAN VIMENTIN COIL...) |
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| - | [[Image:1gk7.gif|left|200px]]<br /> | + | [[Image:1gk7.gif|left|200px]]<br /><applet load="1gk7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gk7" size=" | + | |
caption="1gk7, resolution 1.40Å" /> | caption="1gk7, resolution 1.40Å" /> | ||
'''HUMAN VIMENTIN COIL 1A FRAGMENT (1A)'''<br /> | '''HUMAN VIMENTIN COIL 1A FRAGMENT (1A)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Intermediate filaments (IFs) are key components of the cytoskeleton in | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1GK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Geisler, N.]] | [[Category: Geisler, N.]] | ||
[[Category: Herrmann, H.]] | [[Category: Herrmann, H.]] | ||
| - | [[Category: Strelkov, S | + | [[Category: Strelkov, S V.]] |
[[Category: Zimbelmann, R.]] | [[Category: Zimbelmann, R.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: vimentin]] | [[Category: vimentin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:03 2008'' |
Revision as of 10:51, 21 February 2008
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HUMAN VIMENTIN COIL 1A FRAGMENT (1A)
Contents |
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.
Disease
Known disease associated with this structure: Inflammatory response, modulation of OMIM:[607918]
About this Structure
1GK7 is a Single protein structure of sequence from Homo sapiens with as ligand. 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 Thu Feb 21 12:51:03 2008
