[HTML][HTML] Folding and function of the troponin tail domain: effects of cardiomyopathic troponin T mutations
A Hinkle, LS Tobacman - Journal of Biological Chemistry, 2003 - ASBMB
Troponin contains a globular Ca 2+-binding domain and an elongated tail domain
composed of the N terminus of subunit troponin T (TnT). The tail domain anchors troponin to
tropomyosin and actin, modulates myosin function, and is a site of cardiomyopathy-inducing
mutations. Critical interactions between tropomyosin and troponin are proposed to depend
on tail domain residues 112–136, which are highly conserved across phyla. Most
cardiomyopathy mutations in TnT flank this region. Three such mutations were examined …
composed of the N terminus of subunit troponin T (TnT). The tail domain anchors troponin to
tropomyosin and actin, modulates myosin function, and is a site of cardiomyopathy-inducing
mutations. Critical interactions between tropomyosin and troponin are proposed to depend
on tail domain residues 112–136, which are highly conserved across phyla. Most
cardiomyopathy mutations in TnT flank this region. Three such mutations were examined …