The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study.

Cardiac troponin I, the inhibitory subunit of the heterotrimeric cardiac troponin (cTn) complex is phosphorylated by protein kinase A at two serine residues located in its heart-specific N-terminal extension. This flexible arm interacts at different sites within cTn dependent on its phosphorylation degree. Bisphosphorylation is known to induce conformational changes ...
within cTnI which finally lead to a reduction of the calcium affinity of cTnC. However, as we show here, the bisphosphorylated cTnI arm does not interact with cTnC, but with cTnT and/or cTnI.
Mesh Terms:
Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Myocardium, Phosphorus Isotopes, Phosphorylation, Protein Conformation, Protein Structure, Tertiary, Troponin C, Troponin I, Troponin T
FEBS Lett.
Date: Feb. 27, 2002
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