Why the study?
The study sought to explain the kinetic differences between the skeletal muscle isoform SERCA1a and the heart-specific isoform SERCA2a.
Structural analysis and molecular dynamics simulations reveal that isoform-specific intramolecular interactions may explain the kinetic differences between heart-specific SERCA2a and skeletal muscle SERCA1a.
]E1-AMPPCP form (4.0 Å). The structures are similar to the skeletal muscle isoform SERCA1a pointing to a conserved mechanism. We seek to explain the kinetic differences between SERCA1a and SERCA2a. We find that several isoform-specific residues are acceptor sites for post-translational modifications. In addition, molecular dynamics simulations predict that isoform-specific residues support distinct intramolecular interactions in SERCA2a and SERCA1a. Our experimental observations further indicate that isoform-specific intramolecular interactions are functionally relevant, and may explain the kinetic differences between SERCA2a and SERCA1a.
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Sitsel et al. (2019) studied this question.
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