| pubmed-article:1582406 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1582406 | lifeskim:mentions | umls-concept:C0162340 | lld:lifeskim |
| pubmed-article:1582406 | lifeskim:mentions | umls-concept:C0056248 | lld:lifeskim |
| pubmed-article:1582406 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:1582406 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1582406 | pubmed:dateCreated | 1992-6-16 | lld:pubmed |
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| pubmed-article:1582406 | pubmed:abstractText | Titin is at present the largest known protein (M(r) 3000 kDa) and its expression is restricted to vertebrate striated muscle. Single molecules span from M- to Z-lines and therefore over 1 micron. We have isolated cDNAs encoding five distant titin A-band epitopes, extended their sequences and determined 30 kb (1000 kDa) of the primary structure of titin. Sequences near the M-line encode a kinase domain and are closely related to the C-terminus of twitchin from Caenorhabditis elegans. This suggests that the function of this region in the titin/twitchin family is conserved throughout the animal kingdom. All other A-band sequences consist of 100 amino acid (aa) repeats predicting immunoglobulin-C2 and fibronectin type III globular domains. These domains are arranged into highly ordered 11 domain super-repeat patterns likely to match the myosin helix repeat in the thick filament. Expressed titin fragments bind to the LMM part of myosin and C-protein. Binding strength increases with the number of domains involved, indicating a cumulative effect of multiple binding sites for myosin along the titin molecule. We conclude that A-band titin is likely to be involved in the ordered assembly of the vertebrate thick filament. | lld:pubmed |
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| pubmed-article:1582406 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1582406 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1582406 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1582406 | pubmed:month | May | lld:pubmed |
| pubmed-article:1582406 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1582406 | pubmed:author | pubmed-author:TrinickJJ | lld:pubmed |
| pubmed-article:1582406 | pubmed:author | pubmed-author:LabeitSS | lld:pubmed |
| pubmed-article:1582406 | pubmed:author | pubmed-author:GautelMM | lld:pubmed |
| pubmed-article:1582406 | pubmed:author | pubmed-author:LakeyAA | lld:pubmed |
| pubmed-article:1582406 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1582406 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1582406 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1582406 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1582406 | pubmed:pagination | 1711-6 | lld:pubmed |
| pubmed-article:1582406 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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