title: Spectroscopic studies of phospholamban variants in phospholipid bilayers.
abstract: Phospholamban (PLB) is a 52 amino acid transmembrane protein found in the sarcoplasmic reticulum of cardiac myocytes, where it regulates the transport of calcium ions by SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase). This work has shown that the cytoplasmic domain of PLB associates with phospholipid vesicles, possibly with the lipid polar head groups, and, in doing so, undergoes a transition from a random coil to a more helical conformation. These findings support a recent hypothesis that the cytoplasmic domain of PLB acts as a conformational switch, alternating between an orientation that lies across the membrane surface and an upright orientation that associates with the regulatory site of SERCA.
authors.affiliation: Faculty of Life Sciences, University of Manchester, PO Box 88, Manchester M60 1QD, UK.
authors.forename: J C
authors.initials: JC
authors.lastname: Clayton
authors.forename: E
authors.initials: E
authors.lastname: Hughes
authors.forename: D A
authors.initials: DA
authors.lastname: Middleton
mesh_terms: D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D014644:Genetic Variation; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D000099211:Phospholamban
chemical_list: D002135:Calcium-Binding Proteins; D008051:Lipid Bilayers; D000099211:Phospholamban