Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide

Journal of Biomolecular Structure & Dynamics
H FabianH H Mantsch

Abstract

One of the major immunodominant epitopes of the paired helical filaments (PHF) of Alzheimer's disease is the peptide sequence GAEIVYKSPVVSGD (T3), comprising amino acids 389-402 of the microtubule-associated protein, tau, when it is phosphorylated at the first serine residue. While the corresponding anti-PHF monoclonal antibody recognizes the peptide phosphorylated at either serine, it does not recognize the tyrosine-phosphorylated peptide. Here we describe the effect of serine- versus tyrosine-phosphorylation on the conformation of a synthetic tau peptide. While adding a phosphate to the serine residue has practically no impact on the structure of the non-phosphorylated peptide, phosphorylation of the tyrosine results in considerable conformational changes.

References

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Citations

May 26, 2005·Brain Research. Molecular Brain Research·Irving E VegaShu-Hui Yen
May 23, 2012·PloS One·Zuzana TatárováMarian Novotný
Feb 26, 2016·International Journal of Biological Macromolecules·Kazem AsadollahiMojtaba Falahati
Dec 24, 2004·Biochimica Et Biophysica Acta·Li-Wen KoShu-Hui Yen
Dec 26, 2006·American Journal of Physiology. Lung Cellular and Molecular Physiology·Hephzibah Rani S TagaramJoanna Floros
Jul 18, 1997·The Journal of Biological Chemistry·A NilssonJ F Allen
Jun 27, 2019·Journal of the American Society of Nephrology : JASN·Irini TossidouMario Schiffer

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