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J Biomol Struct Dyn. 1994 Dec;12(3):573-9.

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

Author information

1
Institute for Biochemistry, Humboldt University Berlin, Germany.

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.

PMID:
7537044
DOI:
10.1080/07391102.1994.10508760
[Indexed for MEDLINE]
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