Key result
Cross-linking of the N-terminal extension of human cardiac troponin I revealed specific intramolecular interactions at Met-154 and Met-155 and intermolecular interactions at Met-47 and Met-80 of troponin C.
Population
Reconstituted human cardiac whole troponin complex with single cysteine mutants (hcTnI-S5C and hcTnI-I19C)
Comparison
Labeling with hetero-bifunctional cross-linker… vs Non-labeled troponin
Design
Preclinical
Authors
Loading...
These troponin sites may modulate Ca2+ regulation; leaves open translation to human cardiomyopathy or therapies.
The study identifies specific intra- and intermolecular interaction sites of the human cardiac troponin I N-terminus, revealing different functional effects on Ca2+ regulation depending on the cross-linking site.
Warren et al. (2009) studied this question. Mutant human cardiac troponin I (hcTnI-S5C and hcTnI-I19C) vs. Non-labeled troponin was evaluated on Sites of intra- and intermolecular cross-linking and Ca2+-dependent ATPase rate. Cross-linking of the N-terminal extension of human cardiac troponin I revealed specific intramolecular interactions at Met-154 and Met-155 and intermolecular interactions at Met-47 and Met-80 of troponin C.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: