Premium
The solution structure of the C ‐terminal segment of tau protein
Author(s) -
Esposito G.,
Viglino P.,
Novak M.,
Cattaneo A.
Publication year - 2000
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/1099-1387(200011)6:11<550::aid-psc272>3.0.co;2-s
Subject(s) - tau protein , chemistry , peptide , nuclear magnetic resonance spectroscopy , microtubule , crystallography , structural motif , biophysics , small molecule , stereochemistry , alzheimer's disease , biochemistry , microbiology and biotechnology , biology , disease , medicine , pathology
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 1 H 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 © 2000 European Peptide Society and John Wiley & Sons, Ltd.