Evidence for a phosphorylation‐induced conformational change in phospholamban cytoplasmic domain by CD analysis
- 14 September 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 309 (3), 413-416
- https://doi.org/10.1016/0014-5793(92)80819-3
Abstract
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 peptideKeywords
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