[HTML][HTML] Molecular basis of calmodulin binding to cardiac muscle Ca2+ release channel (ryanodine receptor)
N Yamaguchi, L Xu, DA Pasek, KE Evans… - Journal of Biological …, 2003 - ASBMB
Calmodulin (CaM) is a ubiquitous Ca 2+-binding protein that regulates the ryanodine
receptors (RyRs) by direct binding. CaM inhibits the skeletal muscle ryanodine receptor
(RyR1) and cardiac muscle receptor (RyR2) at> 1 μm Ca 2+ but activates RyR1 and inhibits
RyR2 at< 1 μm Ca 2+. Here we tested whether CaM regulates RyR2 by binding to a highly
conserved site identified previously in RyR1. Deletion of RyR2 amino acid residues 3583–
3603 resulted in background [35 S] CaM binding levels. In single channel measurements …
receptors (RyRs) by direct binding. CaM inhibits the skeletal muscle ryanodine receptor
(RyR1) and cardiac muscle receptor (RyR2) at> 1 μm Ca 2+ but activates RyR1 and inhibits
RyR2 at< 1 μm Ca 2+. Here we tested whether CaM regulates RyR2 by binding to a highly
conserved site identified previously in RyR1. Deletion of RyR2 amino acid residues 3583–
3603 resulted in background [35 S] CaM binding levels. In single channel measurements …