1gk7: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
caption="1gk7, resolution 1.40&Aring;" />
caption="1gk7, resolution 1.40&Aring;" />
'''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, 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==
==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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GK7 OCA].  
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.V.]]
[[Category: Strelkov, S V.]]
[[Category: Zimbelmann, R.]]
[[Category: Zimbelmann, R.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: vimentin]]
[[Category: vimentin]]


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