Abstract:
:Skeletal muscle contraction is regulated by a complex of five polypeptides which are stably associated with the actin filament. This complex consists of two proteins: troponin with three subunits (TnC; TnI and TnT) and tropomyosin (a dimer of two chains). Using deletion mutants of TnC, TnI and TnT we determined that each of these polypeptides can be divided into at least two domains. One domain is responsible for the regulatory properties of the protein. Its interaction with the other components of the system change upon calcium binding to TnC. A second domain present in each of these proteins is responsible for the stable association of the complex to the actin filament. The interactions among this second set of domains is not influenced by calcium binding to TnC. The structural interactions are: 1) interactions between the C-domain of TnC with the N-domain of TnI; 2) interactions of the N-domain of TnI with the C-terminal domain of TnT and 3) interactions between the N-domain of TnT (T1) and actin/tropomyosin.
journal_name
Cell Struct Functjournal_title
Cell structure and functionauthors
Reinach FC,Farah CS,Monteiro PB,Malnic Bdoi
10.1247/csf.22.219subject
Has Abstractpub_date
1997-02-01 00:00:00pages
219-23issue
1eissn
0386-7196issn
1347-3700journal_volume
22pub_type
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