Key result
S16 phosphorylation disrupts the L-shaped structure of monomeric phospholamban, inducing an order-to-disorder transition that decreases its inhibition of SERCA.
Population
Monomeric, fully active mutant of Phospholamban where C36, C41, and C46 have been mutated to A36, F41, and A46
Comparison
Phosphorylation at Serine 16 (S16) vs Unphosphorylated PLB
Design
Preclinical
Authors
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Elucidates phospholamban-SERCA regulation mechanism; leaves open translation to human heart failure therapies.
S16 phosphorylation of phospholamban induces an order-to-disorder structural transition that propagates throughout the protein backbone, providing a mechanistic basis for its decreased inhibition of SERCA.
Metcalfe et al. (2005) studied this question. S16 phosphorylation vs. Unphosphorylated PLB was evaluated on Structural and dynamics changes in monomeric PLB. S16 phosphorylation disrupts the L-shaped structure of monomeric phospholamban, inducing an order-to-disorder transition that decreases its inhibition of SERCA.
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