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PMID: 3134620 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structure and elasticity of microtubule-associated protein tau.

Nature ·Vol. 334 ·No. 6180 ·1988-07-28 ·Pages 359-62

Lichtenberg B, Mandelkow EM, Hagestedt T, Mandelkow E

Abstract

Tau is one of the diverse group of microtubule-associated proteins that bind to microtubules and may thereby influence their structure and function. It occurs in the mammalian brain, mainly in axons, and is a component of the neurofibrillary tangles of Alzheimer's disease. Tau was recently sequenced, but there remains a short-age of structural data on the protein. We have now prepared paracrystals of tau suitable for electron microscopy and image processing. They show distinct transverse banding and polarity, indicating that the protein subunits are aligned with the same orientations. In contrast to other paracrystals, those of tau protein can stretch or contract continuously by more than three-fold; the axial repeats range from 22 to 68 nm. After scaling to a common period, the density distributions are closely superimposable. This suggests that tau is an elastic molecule.

MeSH Terms
Chemical Phenomena Chemistry, Physical Crystallization Macromolecular Substances Microtubule-Associated Proteins Protein Conformation tau Proteins
Chemicals
Macromolecular Substances Microtubule-Associated Proteins tau Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lichtenberg B
Max-Planck-Unit for Structural Molecular Biology, Hamburg, FRG.
Mandelkow E M
Hagestedt T
Mandelkow E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1988-07-28
Pages
359-62
Language
English
Region
England
NLM ID
0410462
Subset
IM
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