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Calmodulin is a small, highly conserved protein that is 148 amino acids long (16.7 kDa). The protein has two approximately symmetrical globular domains (the N- and C- domains) each containing a pair of EF hand motifs [5] separated by a flexible linker region for a total of four Ca 2+ binding sites, two in each globular domain. [6]
Calcium-binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF-hand domain. Extracellular calcium-binding proteins are classified into six groups. [2] Since Ca (2+) is an important second messenger, it can act as an activator or inhibitor in gene transcription.
Calmodulin 1 is a protein in humans that is encoded by the CALM1 gene. [3] Calmodulin [4] plays a role in calcium signal transduction pathways by regulating control of ion channels, enzymes, aquaporins, and other proteins. It functions as a calcium-binding protein that has been grouped into the EF-hand motif found in eukaryotic cells ...
Shows Ca 2+ release from the endoplasmic reticulum through phospholipase C (PLC) pathway. Calcium signaling is the use of calcium ions (Ca 2+) to communicate and drive intracellular processes often as a step in signal transduction. Ca 2+ is important for cellular signaling.
As the cytoplasmic Ca 2+ concentration rises to ~1 μM during systole, [26] Ca 2+ binding to the regulatory domain of cardiac troponin C (cNTnC) is the key event that leads to muscle contraction. Hydrophobic binding of cNTnC to the "switch" region of troponin I, cTnI 148-159 , stabilizes the Ca 2+ -bound open conformation of cNTnC [ 29 ...
TnT is a tropomyosin-binding subunit which regulates the interaction of troponin complex with thin filaments; TnI inhibits ATP-ase activity of acto-myosin; TnC is a Ca 2+-binding subunit, playing the main role in Ca 2+ dependent regulation of muscle contraction.
Thus, rise in extracellular Ca2+ ions may serve to prime the integrin heterodimer. The release of intracellular Ca2+ have been shown to be important for integrin inside-out activation. [16] However, extracellular Ca2+ binding may exert different effects depending on the type of integrin and the cation concentration. [17]
The transmembrane component consists of single chain glycoprotein repeats. [12] Because cadherins are Ca 2+ dependent, they have five tandem extracellular domain repeats that act as the binding site for Ca 2+ ions. [13] Their extracellular domain interacts with two separate trans dimer conformations: strand-swap dimers (S-dimers) and X-dimers. [13]