Key result
The nonphosphorylated cardiac specific amino-terminus of troponin I makes additional interactions with the N-terminal domain of cardiac troponin C compared to phosphorylated states.
Population
Recombinant N-terminal cardiac troponin I proteins and recombinant cardiac troponin C
Comparison
Phosphorylation by protein kinase A or… vs Nonphosphorylated cardiac specific amino-terminus
Design
Preclinical
Authors
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Offers mechanistic insight into troponin regulation but should not change practice; leaves open human validation.
Phosphorylation of cardiac troponin I alters its interaction with the N-terminal domain of cardiac troponin C, providing a structural basis for reduced calcium affinity.
Finley et al. (1999) studied this question. Recombinant N-terminal cardiac troponin I proteins was evaluated on Structural interactions between cardiac troponin I and troponin C. The nonphosphorylated cardiac specific amino-terminus of troponin I makes additional interactions with the N-terminal domain of cardiac troponin C compared to phosphorylated states.
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