Key result
Mono- and consecutive bisphosphorylation of cTnI gradually reduces affinity to cTnC and cTnT by lowering association rate constants, while enhancing dissociation rate constants in ternary complexes.
Mono- and bisphosphorylation of cardiac troponin I induce distinct conformational changes that alter the binding affinities between troponin subunits.
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Hypothesis-generating for cTnI phosphorylation in cardiac regulation; human studies needed before clinical relevance.
Reiffert et al. (1998) studied Cardiac troponin subunit interactions. Mono- and bisphosphorylation of cardiac troponin I (cTnI) vs. Dephospho state was evaluated on Association and dissociation rate constants of binary and ternary troponin complexes. Mono- and consecutive bisphosphorylation of cTnI gradually reduces affinity to cTnC and cTnT by lowering association rate constants, while enhancing dissociation rate constants in ternary complexes.
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