The solution structure of the C-terminal segment of tau protein

G. Esposito, P. Viglino, M. Novak, A. Cattaneo

Research output: Contribution to journalArticlepeer-review

Abstract

Pathological changes in the microtubule associated protein tau, leading to tau-containing filamentous lesions, are a major hallmark common to many types of human neurodegenerative diseases, including Alzheimer's disease (AD). No structural data are available which could rationalize the extensive conformational changes that occur when tau protein is converted to Alzheimer's paired helical filaments (PHF). The C-terminal portion of tau plays a crucial role in the aggregation of tau into PHF and in the truncation process that generates cytotoxic segments of tau. Therefore, we investigated the solution structure of the hydrophobic C-terminal segment 423-441 of tau protein (PQLATLADEVSASLAKQGL) by 1H 2D NMR spectroscopy. The peptide displays the typical NMR evidence consistent with a α-helix geometry with a stabilizing C-capping motif. The reported data represent the first piece of structural information on an important portion of the molecule and can have implications towards the understanding of its pathophysiology. Copyright (C) 2000 European Peptide society and John Wiley and Sons, Ltd.

Original languageEnglish (US)
Pages (from-to)550-559
Number of pages10
JournalJournal of Peptide Science
Volume6
Issue number11
DOIs
StatePublished - 2000

Keywords

  • Alzheimer's disease
  • C-capping
  • Helix capping
  • NMR of peptides
  • NMR structure
  • Protection from proteolysis
  • Tau protein
  • α-helix conformation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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