Journal article
NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation
FEBS letters, Vol.453(1), pp.107-112
1999
Handle:
https://hdl.handle.net/2376/115360
PMID: 10403385
Abstract
Phosphorylation of the cardiac specific amino-terminus of troponin I has been demonstrated to reduce the Ca
2+ 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.
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Details
- Title
- NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation
- Creators
- Natosha Finley - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAM.Bret Abbott - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAEkram Abusamhadneh - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAVadim Gaponenko - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAWen-ji Dong - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAG Gasmi-Seabrook - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAJack W Howarth - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAMark Rance - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USAR.John Solaro - Department of Physiology and Biophysics, College of Medicine, University of Illinois, Chicago, IL 60612, USAHerbert C Cheung - Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294, USAPaul R Rosevear - Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267, USA
- Publication Details
- FEBS letters, Vol.453(1), pp.107-112
- Academic Unit
- Chemical Engineering and Bioengineering, School of
- Publisher
- Elsevier B.V
- Identifiers
- 99900547840401842
- Language
- English
- Resource Type
- Journal article