Ontology highlight
ABSTRACT:
SUBMITTER: Newman RA
PROVIDER: S-EPMC4208696 | biostudies-literature | 2014 Sep-Oct
REPOSITORIES: biostudies-literature
Newman Rhonda A RA Sorensen Brenda R BR Kilpatrick Adina M AM Shea Madeline A MA
Biophysical chemistry 20140730
Calmodulin (CaM) allosterically regulates the homo-tetrameric human Ryanodine Receptor Type 1 (hRyR1): apo CaM activates the channel, while (Ca(2+))4-CaM inhibits it. CaM-binding RyR1 residues 1975-1999 and 3614-3643 were proposed to allow CaM to bridge adjacent RyR1 subunits. Fluorescence anisotropy titrations monitored the binding of CaM and its domains to peptides encompassing hRyR(11975-1999) or hRyR1(3614-3643). Both CaM and its C-domain associated in a calcium-independent manner with hRyR1 ...[more]