Key result
Metal binding to the NH2-terminal extension of slow skeletal muscle troponin T induced conformational changes affecting its interaction with troponin I, troponin C, and tropomyosin.
Population
Recombinant protein model
Design
Preclinical
Authors
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Does not support clinical translation in muscle disorders; leaves open troponin T metal-binding roles in humans.
The NH2-terminal metal-binding extension confers specific conformational modulation in slow skeletal muscle TnT, altering its interactions with key regulatory proteins.
Jin et al. (2000) studied this question. Recombinant protein with metal-binding peptide fused to NH2 terminus of mouse slow skeletal muscle TnT was evaluated on Conformational changes and protein binding interactions. Metal binding to the NH2-terminal extension of slow skeletal muscle troponin T induced conformational changes affecting its interaction with troponin I, troponin C, and tropomyosin.
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