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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2002-3-12
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/PDB/1AA0,
http://linkedlifedata.com/resource/pubmed/xref/PDB/1GK4,
http://linkedlifedata.com/resource/pubmed/xref/PDB/1GK6,
http://linkedlifedata.com/resource/pubmed/xref/PDB/1GK7,
http://linkedlifedata.com/resource/pubmed/xref/PDB/2ZTA,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P02545,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P05783,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P05787,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P07196,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08670,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P17661,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P20700
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10064706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10518990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10679360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10745004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10801351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-10845237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11014182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11029054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11030624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11156599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11165516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11166216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-11243787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-1370491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-1376637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-1606966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-1948029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-2417512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-6202512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-7527050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-7531336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-7693709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-7979242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8167022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8210313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8320262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8769421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8913681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8916221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-8918191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9000622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9261070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9614936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9631290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9761844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9828010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11889032-9932497
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1255-66
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11889032-Amino Acid Sequence,
pubmed-meshheading:11889032-Conserved Sequence,
pubmed-meshheading:11889032-Crystallography, X-Ray,
pubmed-meshheading:11889032-Dimerization,
pubmed-meshheading:11889032-Humans,
pubmed-meshheading:11889032-Intermediate Filaments,
pubmed-meshheading:11889032-Models, Molecular,
pubmed-meshheading:11889032-Molecular Sequence Data,
pubmed-meshheading:11889032-Protein Structure, Secondary,
pubmed-meshheading:11889032-Sequence Homology, Amino Acid,
pubmed-meshheading:11889032-Vimentin
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pubmed:year |
2002
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pubmed:articleTitle |
Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly.
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pubmed:affiliation |
Maurice E.Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. sergei-v.strelkov@unibas.ch
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