Abstract
We are studying the structural dynamics of phospholamban (PLB), a regulator of the SR calcium ATPase (SERCA), by combining site-directed spin-labeling and EPR spectroscopy with solid-phase peptide synthesis. PLB is a 52-residue integral membrane protein that binds and inhibits SERCA in the presence of sub-micromolar calcium concentrations. SERCA activity can be restored without dissociating the two proteins by phosphorylating PLB at Ser16 (Mueller et al., 2004). To observe the effects of phosphorylation and SERCA-binding on PLB conformation, we have synthesized PLB analogs containing the spin-labeled amino acid TOAC.
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