Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy.
The neuronal Tau protein, whose physiological role is to stabilize the microtubules, is found under the form of aggregated filaments and tangles in Alzheimer's diseased neurons. Until recently detailed structural analysis of the natively unfolded Tau protein has been hindered due to its shear size and unfavourable amino acid composition. We review here the recent progress in the assignments of the full-length polypeptide using novel methods of product planes and peptide NMR mapping, and indicate the structural insights that can be obtained from this assignment. Preliminary NMR data on the fibers show that the assignment enables a precise mapping of the rigid core. Future NMR experiments should allow one to gain more insight into the conformational aspects of this intriguing protein.
Lippens
Guy
G
CNRS-Université de Lille2 UMR 8525, Institut Pasteur de Lille, 1 rue du Professeur Calmette, BP 245, 59019 Lille Cedex France. guy.lippens@pasteur-lille.fr
Sillen
Alain
A
Smet
Caroline
C
Wieruszeski
Jean-Michel
JM
Leroy
Arnaud
A
Buée
Luc
L
Landrieu
Isabelle
I
D000544:Alzheimer Disease / Q000378:metabolism; D005544:Forecasting; D006801:Humans; D009474:Neurons / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D016875:tau Proteins