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A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
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of special interest, of outstanding interest. Another study of pentamer stability by mutagenesis of the transmembrane domain. Full-length PLB is expressed, in this case, and the pattern of disruptive residues is similar to that of Arkin et al. [19]. The archetypic leucine zipper is used as a basis for the model of a five-stranded coiled coil. As a result, the rotational orientation of helices within the coiled coil are different than those of Adams et al. [20] by 45° but consistent with the X-ray structure of a structurally related coiled coil by Malashkevich et al. [23].
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of special interest. COMP is functionally unrelated to PLB but forms a five-stranded coiled coil and shows exactly the same pattern of leucine and isoleucine residues that stabilize the PLB pentamer. Thus, this structure is likely to be close to that of the transmembrane domain of PLB.
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Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? of special interest Science. 274:1996;761-765 COMP is functionally unrelated to PLB but forms a five-stranded coiled coil and shows exactly the same pattern of leucine and isoleucine residues that stabilize the PLB pentamer. Thus, this structure is likely to be close to that of the transmembrane domain of PLB.
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of special interest. This first study of the oligomeric state of PLB in the membrane. EPR is used to identify a population of less mobile lipids, which are considered to be boundary lipids. On the basis of geometrical considerations, the ratio of boundary lipids to bulk lipids is then used to estimate the oligomeric state of PLB. Consistent with results from SDS-PAGE, wild-type PLB is found to be oligomeric, albeit with only 3.5 monomers per oligomer, and the mutant Leu37→Ala is monomeric. Interestingly, phosphorylation drives both of these PLBs to a higher oligomeric state (the wild-type to a pentamer and the Leu37→Ala mutant to a dimer).
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Cornea RL, Jones LR, Autry JM, Thomas DD. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. of special interest Biophys J. 36:1997;2960-2967 This first study of the oligomeric state of PLB in the membrane. EPR is used to identify a population of less mobile lipids, which are considered to be boundary lipids. On the basis of geometrical considerations, the ratio of boundary lipids to bulk lipids is then used to estimate the oligomeric state of PLB. Consistent with results from SDS-PAGE, wild-type PLB is found to be oligomeric, albeit with only 3.5 monomers per oligomer, and the mutant Leu37→Ala is monomeric. Interestingly, phosphorylation drives both of these PLBs to a higher oligomeric state (the wild-type to a pentamer and the Leu37→Ala mutant to a dimer).
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