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- W3200156731 abstract "Mutations in the cardiac ryanodine receptor type 2 (RyR2) have been linked to a variety of cardiac arrhythmias, such as catecholaminergic polymorphic ventricular tachycardia (CPVT). RyR2 is regulated by calmodulin (CaM), and mutations that disrupt their interaction can cause aberrant calcium release, leading to an arrhythmia. It was recently shown that increasing the RyR2-CaM binding affinity could rescue a defective CPVT-related RyR2 channel to near wild-type behavior. However, the interactions that determine the binding affinity at the RyR2-CaM binding interface are not well understood. In this study, we identify the key domains and interactions, including several new interactions, involved in the binding of CaM to RyR2. Also, our comparison between the wild-type and V3599K mutant suggests how the RyR2-CaM binding affinity can be increased via a change in the central and N-terminal lobe binding contacts for CaM. This computational approach provides new insights into the effect of a mutation at the RyR2-CaM binding interface, and it may find utility in drug design for the future treatment of cardiac arrhythmias." @default.
- W3200156731 created "2021-09-27" @default.
- W3200156731 creator A5044079903 @default.
- W3200156731 creator A5068949499 @default.
- W3200156731 creator A5078091958 @default.
- W3200156731 creator A5083684380 @default.
- W3200156731 date "2021-09-17" @default.
- W3200156731 modified "2023-09-23" @default.
- W3200156731 title "Computational Analysis of Binding Interactions between the Ryanodine Receptor Type 2 and Calmodulin" @default.
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- W3200156731 doi "https://doi.org/10.1021/acs.jpcb.1c03896" @default.
- W3200156731 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34533024" @default.
- W3200156731 hasPublicationYear "2021" @default.
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