Ca2+ regulation of contraction in vertebrate striated muscle is exerted primarily through
effects on the thin filament, which regulate strong cross-bridge binding to actin. Structural …

The calcium binding proteins of the EF-hand super-family are involved in the regulation of all
aspects of cell function. These proteins exhibit a great diversity of composition, structure …

The binding of a new calcium sensitizer, levosimendan, to human cardiac troponin C (cTnC)
is described. Fluorescence studies done on dansylated recombinant human cTnC and a site …

This review discusses the structure and properties of the isolated components of troponin,
their interaction, and the mechanisms of regulation of contractile activity of skeletal and …

Publisher Summary This chapter describes and compares the calcium (Ca 2+)-binding sites
in proteins, attempting to extract common features from them. It determines the functional …

Calcium binding to regulatory sites located in the NH2-terminal domain of troponin C (TnC)
induces a conformational change that blocks the inhibitory action of troponin I (TnI) and …

To investigate the functional importance of the C-terminal residues 116 to 148 of troponin I
(TnI) in the Ca2+-dependent regulation of vertebrate skeletal muscle contraction, we have …

Molecular Genetic Analysis of Muscle Development, Structure, and Function in Drosophila -
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Abstract Background: In contrast to Ca 2+ 4-bound calmodulin (CaM), which has evolved to
bind to many target sequences and thus regulate the function of a variety of enzymes …

Cardiac troponin C belongs to the EF-hand superfamily of calcium-binding proteins and
plays an essential role in the regulation of muscle contraction and relaxation. To follow …