[HTML][HTML] Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor
T Wagenknecht, M Radermacher, R Grassucci… - Journal of Biological …, 1997 - ASBMB
Isolated skeletal muscle ryanodine receptors (RyRs) complexed with the modulatory
ligands, calmodulin (CaM) or 12-kDa FK506-binding protein (FKBP12), have been
characterized by electron cryomicroscopy and three-dimensional reconstruction. RyRs are
composed of 4 large subunits (molecular mass 565 kDa) that assemble to form a 4-fold
symmetric complex that, architecturally, comprises two major substructures, a large (≈ 80%
of the total mass) cytoplasmic assembly and a smaller transmembrane assembly. Both CaM …
ligands, calmodulin (CaM) or 12-kDa FK506-binding protein (FKBP12), have been
characterized by electron cryomicroscopy and three-dimensional reconstruction. RyRs are
composed of 4 large subunits (molecular mass 565 kDa) that assemble to form a 4-fold
symmetric complex that, architecturally, comprises two major substructures, a large (≈ 80%
of the total mass) cytoplasmic assembly and a smaller transmembrane assembly. Both CaM …