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Structural And Dynamic Basis Of Phospholamban And Sarcolipin Inhibition Of Ca2+-Atpase, Nathaniel J. Traaseth, Kim N. Ha, Raffaello Verardi, Lei Shi, Jarrod J. Buffy, Larry R. Masterson, Gianluigi Veglia
Structural And Dynamic Basis Of Phospholamban And Sarcolipin Inhibition Of Ca2+-Atpase, Nathaniel J. Traaseth, Kim N. Ha, Raffaello Verardi, Lei Shi, Jarrod J. Buffy, Larry R. Masterson, Gianluigi Veglia
Larry Masterson
Phospholamban (PLN) and sarcolipin (SLN) are two single-pass membrane proteins that regulate Ca2+-ATPase (SERCA), an ATP-driven pump that translocates calcium ions into the lumen of the sarcoplasmic reticulum, initiating muscle relaxation. Both proteins bind SERCA through intramembrane interactions, impeding calcium translocation. While phosphorylation of PLN at Ser-16 and/or Thr-17 reestablishes calcium flux, the regulatory mechanism of SLN remains elusive. SERCA has been crystallized in several different states along the enzymatic reaction coordinates, providing remarkable mechanistic information; however, the lack of high-resolution crystals in the presence of PLN and SLN limits the current understanding of the regulatory mechanism. This …