NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation
| Autor: | Ekram Abusamhadneh, M. Bret Abbott, R. John Solaro, Vadim Gaponenko, Wen-Ji Dong, Herbert C. Cheung, Genevieve Gasmi-Seabrook, Mark Rance, Paul R. Rosevear, Natosha Finley, Jack W. Howarth |
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| Jazyk: | angličtina |
| Předmět: |
Molecular Sequence Data
Biophysics macromolecular substances Biochemistry Protein Structure Secondary law.invention Troponin C Protein structure Troponin complex Structural Biology law Troponin I Genetics Amino Acid Sequence Phosphorylation Protein kinase A Molecular Biology Nuclear Magnetic Resonance Biomolecular Troponin T Chemistry Myocardium Cardiac troponin I Cardiac troponin C Cell Biology Phosphoproteins musculoskeletal system Molecular biology NMR Mutagenesis Recombinant DNA cardiovascular system Isotope labelling Protein Binding |
| Zdroj: | FEBS Letters. (1-2):107-112 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(99)00693-6 |
| Popis: | 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 non-phosphorylated 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: | OpenAIRE |
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