Evidence for a phosphorylation‐induced conformational change in phospholamban cytoplasmic domain by CD analysis

FEBS Letters

Terzi, Evelyne¹  Trifilieff, Elisabeth¹  Poteur, Livia¹ 

[1] Laboratoire de Chimie Organique des Substances Naturelles, CNRS URA 31, 5 Rue Blaise Pascal, 67084-Strasbourg Cedex, France

关键词: Phospholamban;    Synthetic peptide;    Phosphorylation;    Circular dichroism;    PLB;    phospholamban;    SR;    sarcoplasmic reticulum;    CD;    circular dichroism;    Boc;    tert-butyloxycarbonyl;    BOP;    benzotriazoyl-N-oxy-tris (dimethylamino) phosphonium hexafluorophosphate;    DIEA;    N-ethyl-diisopropylamine;    DCM;    dichloromethane;    DMF;    dimethylformamide;    HF;    hydrogen fluoride;    TFE;    trifluoroethanol;    FAB-MS;    fast atom bombardment mass spectrometry;   

DOI  :  10.1016/0014-5793(92)80819-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phospholamban (PLB), an integral membrane protein of cardiac sarcoplasmic reticulum (SR), is described as the regulator of the Ca²⁺-ATPase pump, via its phosphorylation-dephosphorylation of Ser-16. Recently it has been shown that a direct interaction between the N-terminal hydrophilic domain of PLB and Ca²⁺-ATPase may be one of the mechanisms of regulation. In order to show that this interaction could be modulated by a phosphorylation-induced conformational change in PLB, we ran CD studies on the synthetic peptide PLB(2-33) in its phosphorilated and non-phosphorylated forms, at various pHs, concentrations and in the absence or presence of trifluoroethanol. The results show a clear difference in structure of the phosphorylated and non-phosphorylated peptide.

【 授权许可】

Unknown