Key result
A recombinant deletion mutant of rabbit fast skeletal muscle troponin I lacking residues 1-57 retained inhibitory actin binding but lost Ca2+-Mg2+-dependent binding to TnC.
Population
Rabbit fast skeletal muscle troponin I and recombinant deletion mutant expressed in a bacterial system
Comparison
Recombinant deletion mutant lacking residues 1-57 vs Wild type TnI (WTnI)
Design
Preclinical
Authors
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Does not inform clinical practice; extends mapping of TnI NH2-terminus interactions in skeletal muscle.
The NH2 terminus of fast skeletal muscle troponin I plays a structural role and mediates Ca2+-Mg2+-dependent interactions with troponin C.
Sheng et al. (1992) studied this question. Recombinant deletion mutant (TnId57) lacking residues 1-57 vs. Wild type TnI (WTnI) was evaluated on Interaction between TnC and TnI (acto-S1-ATPase activity inhibition, actin binding, TnC affinity). A recombinant deletion mutant of rabbit fast skeletal muscle troponin I lacking residues 1-57 retained inhibitory actin binding but lost Ca2+-Mg2+-dependent binding to TnC.
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