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Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain.

Sia SK, Li MX, Spyracopoulos L, Gagné SM, Liu W, Putkey JA, Sykes BD
J Biol Chem 272 18216-21 (1997)
Related entries: 1aj4, 2ctn

Cited: 109 times
EuropePMC logo PMID: 9218458

Abstract

The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.

Articles - 3ctn mentioned but not cited (5)

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  5. Minding the gaps: assessing and addressing clinical research core competencies across a network of Canadian cancer centres. Sundquist S, Kato D, Chowdhury R, Samara C, Dancey JE. Front Pharmacol 14 1294335 (2023)


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Articles citing this publication (84)

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