Structural principles of tau and the paired helical filaments of Alzheimer's disease.
Tau, a major microtubule-associated protein in brain, forms abnormal fibers in Alzheimer's disease and several other neurodegenerative diseases. Tau is highly soluble and adopts a natively unfolded structure in solution. In the paired helical filaments of Alzheimer's disease, small segments of tau adopt a beta-conformation and interact with other tau molecules. In the filament core, the microtubule-binding repeat region of tau has a cross-beta structure, while the rest of the protein retains its largely unfolded structure and gives rise to the fuzzy coat of the filaments.
Mandelkow
Eckhard
E
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. mand@mpasmb.desy.de
von Bergen
Martin
M
Biernat
Jacek
J
Mandelkow
Eva-Maria
EM
D000544:Alzheimer Disease / Q000378:metabolism*; D006801:Humans; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
D016875:tau Proteins