JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
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Modulation of cardiac ryanodine receptor 2 by calmodulin.

Nature 2019 August
The high-conductance intracellular calcium (Ca2+ ) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca2+ -dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca2+ -CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca2+ binding to CaM, rather than to RyR2. Ca2+ -CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca2+ -activated channel. By contrast, the pore of the ATP, caffeine and Ca2+ -activated channel remains open in the presence of Ca2+ -CaM, which suggests that Ca2+ -CaM is one of the many competing modulators of RyR2 gating.

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