Structural and Functional Consequences of the Cardiac Troponin C L48Q Ca 2+ -Sensitizing Mutation

  • Wang D
  • Robertson I
  • Li M
 et al. 
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Calcium binding to the regulatory domain of cardiac troponin C (cNTnC) causes a conformational change that exposes a hydrophobic surface to which troponin I (cTnI) binds, prompting a series of protein–protein interactions that culminate in muscle contraction. A number of cTnC variants that alter the Ca2+ sensitivity of the thin filament have been linked to disease. Tikunova and Davis engineered a series of cNTnC mutations that altered Ca2+ binding properties and studied the effects on the Ca2+ sensitivity of the thin filament and contraction [Tikunova, S. B., and Davis, J. P. (2004) J. Biol. Chem. 279, 35341–35352]. One of the mutations they engineered, the L48Q variant, resulted in a pronounced increase in the cNTnC Ca2+ binding affinity and Ca2+ sensitivity of cardiac muscle force development. In this work, we sought structural and mechanistic explanations for the increased Ca2+ sensitivity of contraction for the L48Q cNTnC variant, using an array of biophysical techniques. We found that the L48Q mutati...

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  • D. Wang

  • I. M. Robertson

  • M. X. Li

  • M. E. Mccully

  • M. L. Crane

  • Z. Luo

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