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[Troponin from the myocardium and skeletal muscles: structure and properties]статья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Автор: Gusev N.B.
- Журнал: Biokhimii∎a (Moscow, Russia)
- Том: 51
- Номер: 12
- Год издания: 1986
- Издательство: IZDATELSTVO NAUKA
- Местоположение издательства: LENINGRADSKOE OTDELENIE MAKAROVA D4, STPETERSBURG, RUSSIA
- Первая страница: 1993
- Последняя страница: 2009
- Аннотация: The literary and experimental data on the structure and properties of cardiac and skeletal muscle troponin are reviewed. The cation--binding sites of cardiac and skeletal muscle troponin C are distinguished by specificity; the sites localized in the C-terminal part of the protein molecule can bind both Ca2+ and Mg2+, whereas the sites localized at the N-end specifically bind Ca2+. The use of bifunctional reagents revealed a number of helical sites within the structure of cardiac troponin C (residues 84-92 and 150-158) and of skeletal muscle troponin C (residues 90-98 and 125-136). A comparison of experimental data with the results of an X-ray analysis testifies to the presence in the central part of the troponin C molecule of a long alpha-helical sequence responsible for troponin C interaction with the inhibiting peptide of troponin I. The efficiency of interaction of troponin components depends on Ca2+ concentration; the integrity of the overall troponin complex is mainly provided for by troponin C interaction with troponin I and by troponin I interaction with troponin T. The interaction between troponins T and C is relatively weak, especially in the case of cardiac troponin components. Both skeletal and cardiac muscles synthesize several troponin T isoforms differing in length and amino acid composition of N-terminal 40-60 member peptides. Troponin T isoforms can undergo phosphorylation by several protein kinases. The single site of troponin T which exists in a phosphorylated state in vivo (residue Ser-1) undergoes phosphorylation by specific protein kinase (troponin T kinase) related to casein kinases II. It was assumed that the phosphorylation of Ser-1 residue of troponin T as well as the synthesis of troponin T isoforms differing in the structure of the N-terminal peptide, provides for the regulation of interaction between two neighbouring tropomyosin molecules.
- Добавил в систему: Гусев Николай Борисович