Abstract
Calmodulin (CaM), a 16 kDa ubiquitous calcium-sensing protein, is known to bind tightly to the cardiac calcium release channel/ryanodine receptor (RyR2) at low and high Ca2+ concentrations, and modulate the function of the channel. CaM binding studies using RyR fragments or synthetic peptides have revealed that multiple regions in the RyR's primary sequence may be involved in CaM binding. However, the locations of these potential CaM binding regions in the three dimensional structure of RyRs have yet to be determined.
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