Structural perspectives of phospholamban, a helical transmembrane pentamer.
Phospholamban is a 52-amino-acid protein that assembles into a pentamer in sarcoplasmic reticulum membranes. The protein has a role in the regulation of the resident calcium ATPase through an inhibitory association that can be reversed by phosphorylation. The phosphorylation of phospholamban is initiated by beta-adrenergic stimulation, identifying phospholamban as an important component in the stimulation of cardiac activity by beta-agonists. In this role of phospholamban that has motivated studies in recent decades. There is evidence that phospholamban may also function as a Ca(2+)-selective ion channel. The structural properties of phospholamban have been studied by mutagenesis, modeling, and spectroscopy, resulting in a new view of the organization of this key molecule in membranes.
Arkin
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Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.
Adams
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Brünger
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Smith
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Engelman
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D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D000099211:Phospholamban