| Autor: |
Finley N; Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, OH 45267, USA., Abbott MB, Abusamhadneh E, Gaponenko V, Dong W, Gasmi-Seabrook G, Howarth JW, Rance M, Solaro RJ, Cheung HC, Rosevear PR |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1999 Jun 18; Vol. 453 (1-2), pp. 107-12. |
| DOI: |
10.1016/s0014-5793(99)00693-6 |
| Abstrakt: |
Phosphorylation of the cardiac specific amino-terminus of troponin I has been demonstrated to reduce the Ca2+ affinity of the cardiac troponin C regulatory site. Recombinant N-terminal cardiac troponin I proteins, cardiac troponin I(33-80), cardiac troponin I(1-80), cardiac troponin I(1-80)DD and cardiac troponin I(1-80)pp, phosphorylated by protein kinase A, were used to form stable binary complexes with recombinant cardiac troponin C. Cardiac troponin I(1-80)DD, having phosphorylated Ser residues mutated to Asp, provided a stable mimetic of the phosphorylated state. In all complexes, the N-terminal domain of cardiac troponin I primarily makes contact with the C-terminal domain of cardiac troponin C. The nonphosphorylated cardiac specific amino-terminus, cardiac troponin I(1-80), was found to make additional interactions with the N-terminal domain of cardiac troponin C. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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