Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket

Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket

<p dir="ltr">Calmodulin (CaM) modulates the activity of several proteins that play a key role in excitation-contraction coupling (ECC). In cardiac muscle, the major binding partner of CaM is the type-2 ryanodine receptor (RyR2) and altered CaM binding contributes to defects in sarcop...

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Bibliographic Details
Main Author: Angelos Thanassoulas (2822861) (author)
Other Authors: Vyronia Vassilakopoulou (17807600) (author), Brian L. Calver (17807603) (author), Luke Buntwal (17807606) (author), Adrian Smith (2385022) (author), Christopher Lai (144808) (author), Iris Kontogianni (17807609) (author), Evangelia Livaniou (2528806) (author), George Nounesis (2202139) (author), F. Anthony Lai (17714499) (author), Michail Nomikos (17563188) (author)
Published: 2023
Subjects:
Biological sciences
Biochemistry and cell biology
Biomedical and clinical sciences
Cardiovascular medicine and haematology
Calmodulin
Ryanodine receptor
RyR2
Arrhythmias
Cardiac disease
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