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Evidence for a phosphorylation‐induced conformational change in phospholamban cytoplasmic domain by CD analysis
Author(s) -
Terzi Evelyne,
Poteur Livia,
Trifilieff Elisabeth
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80819-3
Subject(s) - phospholamban , phosphorylation , dephosphorylation , chemistry , endoplasmic reticulum , peptide , conformational change , biophysics , cytoplasm , atpase , biochemistry , microbiology and biotechnology , biology , phosphatase , enzyme
Phospholamban (PLB), an integral membrane protein of cardiac sarcoplasmic reticulum (SR), is described as the regulator of the Ca 2+ ‐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 Ca 2+ ‐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.