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

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DOIResolve DOI: http://doi.org/10.1080/07391102.1994.10508760
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TypeArticle
Journal titleJournal of Biomolecular Structure and Dynamics
ISSN0739-1102
1538-0254
Volume12
Issue3
Pages573579; # of pages: 7
AbstractOne of the major immunodominant epitopes of the paired helical filaments (PHF) of Alzheimer's disease is the peptide sequence GAEIVYKSPWSGD (T3), comprising amino acids 389–402 of the microtubule-associated protein, τ, 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.
Publication date
PublisherTaylor & Francis Group
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada
Peer reviewedYes
NRC number155
NPARC number9148336
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Record identifierc7074087-59f3-405a-b800-9ceacf4a516b
Record created2009-06-25
Record modified2016-12-05
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