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Troponin T (blue) anchors the complex on tropomyosin. Troponin is found in both skeletal muscle and cardiac muscle, but the specific versions of troponin differ between types of muscle. The main difference is that the TnC subunit of troponin in skeletal muscle has four calcium ion-binding sites, whereas in cardiac muscle there are only three.
Troponin C is a protein which is part of the troponin complex. It contains four calcium-binding EF hands , although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments , along with actin and tropomyosin .
The calcium sensitizer, levosimendan, is purported to bind to troponin C, but only weak or inconsistent binding has been detected, [57] [58] [59] precluding any structure determination. In contrast, levosimendan inhibits type 3 phosphodiesterase with nanomolar affinity, [ 60 ] so its biological target is controversial.
Troponin (Tn), is a key protein complex in the regulation of striated muscle contraction, composed of three subunits. The TnI subunit inhibits actomyosin ATPase , the TnT subunit binds tropomyosin and TnC, while the TnC subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin thin filaments .
Calcium sensitizers function by binding to cardiac troponin C, thereby enhancing the sensitivity of heart muscle cells to naturally occurring calcium ions. [51] This heightened sensitivity fosters a more efficient interaction between calcium and the contractile apparatus of the heart muscle. [52]
Figure 1: Calcium binding to troponin, exposes sites on the actin filaments, to which myosin binds. Using ATP, myosin moves the actin along. The myosin releases the actin, resets itself and binds to another actin binding site. The increase in Ca 2+, produced by CICR, now does two things.
This gene encodes an intracellular calcium-binding protein belonging to the troponin C superfamily. Members of this protein family have six EF-hand domains which bind calcium. This protein plays a role in diverse cellular functions, including message targeting and intracellular calcium buffering. [6]
Troponin I prevents myosin from binding to actin in relaxed muscle. When calcium binds to the troponin C, it causes conformational changes which lead to dislocation of troponin I. Afterwards, tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle. The letter I is given due to its inhibitory character.