Source:http://linkedlifedata.com/resource/pubmed/id/12446666
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2003-1-20
|
| pubmed:abstractText |
Telethonin interacts specifically with the two Z-disk IG-like domains (Z1Z2) at the N terminus of titin, the largest presently known protein. Analytical ultracentrifugation and synchrotron radiation x-ray scattering were employed to study the solution structures of Z1Z2 and its complexes with telethonin, and low resolution models were constructed ab initio from the scattering data. A seven residues-long polyhistidine tag was localized at the tip of the Z1 domain by comparison of independent models of native and His-tagged versions of Z1Z2. The stoichiometry and shape of the complex between the telethonin construct lacking the C terminus and Z1Z2 indicate antiparallel association of two Z1Z2 molecules with telethonin acting as a central linker. The complex of full-length telethonin with Z1Z2 appears to also have a 1:2 stoichiometry at concentrations below 1 mg/ml but dimerizes at higher concentrations. These results suggest a possible role of telethonin in linking titin filaments at the Z-disk periphery.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
278
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2636-44
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:12446666-Cloning, Molecular,
pubmed-meshheading:12446666-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12446666-Escherichia coli,
pubmed-meshheading:12446666-Humans,
pubmed-meshheading:12446666-Models, Molecular,
pubmed-meshheading:12446666-Models, Statistical,
pubmed-meshheading:12446666-Muscle Proteins,
pubmed-meshheading:12446666-Muscles,
pubmed-meshheading:12446666-Mutagenesis, Site-Directed,
pubmed-meshheading:12446666-Protein Binding,
pubmed-meshheading:12446666-Protein Kinases,
pubmed-meshheading:12446666-Protein Structure, Tertiary,
pubmed-meshheading:12446666-Scattering, Radiation,
pubmed-meshheading:12446666-Statistics as Topic,
pubmed-meshheading:12446666-Synchrotrons,
pubmed-meshheading:12446666-Two-Hybrid System Techniques,
pubmed-meshheading:12446666-Ultracentrifugation,
pubmed-meshheading:12446666-X-Rays
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Solution scattering suggests cross-linking function of telethonin in the complex with titin.
|
| pubmed:affiliation |
European Molecular Biology Laboratory (EMBL), Hamburg Outstation, EMBL c/o Deutsches Electronen- Synchrotron (DESY), Notkestrasse 85, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|