The secondary structure of phospholamban: a two-dimensional NMR study.
Phospholamban (PLN) is an intrinsic membrane protein of 52 amino acids which regulates the Ca2+ pump of the sarcoplasmic reticulum of heart, slow-twitch and smooth muscle (SR): it is normally assumed to exist in the membrane as a homopentamer. A monomeric analogue of phospholamban PLN(C41F), in which Cys41 was replaced by a Phe, was synthesized and its conformation studied by 1H NMR spectroscopy in a 1:1 mixture of chloroform/methanol. Most of the resonances in the 1H NMR spectra were assigned. The work has shown that the C-terminal hydrophobic portion forms a very stable alpha-helix. The hydrophilic N-terminal part adopts an alpha-helix configuration which is much less stable except for the stretch containing the phosphorylation sites.
Maslennikov
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IV
Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Sobol
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AG
Anagli
J
J
James
P
P
Vorherr
T
T
Arseniev
A S
AS
Carafoli
E
E
D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry; D017433:Protein Structure, Secondary; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D010750:Phosphoproteins; D000099211:Phospholamban