Abstract
The activity of cardiac ryanodine receptor type 2 (RyR2), a key player in cardiac contractility, is modulated by various post-translational modifications including phosphorylation at three key residues: S2808, S2814, and S2030. Out of these, two residues (S2808 and S2814) lie in a highly flexible loop of the phosphorylation (P2) domain which has remained unresolved in full-length RyR and in crystal structures of the P2 domain alone. This domain faces the inter-subunit interface near the corner of the square prism-shaped cytoplasmic assembly.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
