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Cited by 218

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Domain Conformation of Tau Protein Studied by Solution Small-Angle X-ray Scattering

Mylonas, Efstratios, Hascher, Antje, Bernadó, Pau, Blackledge, Martin, Mandelkow, Eckhard, Svergun, Dmitri I.·2008·Biochemistry
DOI 10.1021/bi800900d
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Abstract

Tau is one of the two main proteins involved in the pathology of Alzheimer's disease via formation of beta-sheet rich intracellular aggregates named paired helical filaments (PHFs). Given that tau is a natively unfolded protein with no folded core (even upon binding to physiological partners such as microtubules), its structural analysis by high-resolution techniques has been difficult. In this study, employing solution small-angle X-ray scattering from the full length isoforms and from a variety of deletion and point mutants the conformation of tau in solution is structurally characterized. A recently developed ensemble optimization method was employed to generate pools of random models and to select ensembles of coexisting conformations, which fitted simultaneously the scattering data from the full length protein and deletion mutants. The analysis of the structural properties of these selected ensembles allowed us to extract information about residual structure in different domains of the native protein. The short deletion mutants containing the repeat domain (considered the core constituent of the PHFs) are significantly more extended than random coils, suggesting an extended conformation of the repeat domain. The longer tau constructs are comparable in size with the random coils, pointing to long-range contacts between the N- and C-termini compensating for the extension of the repeat domain. Moreover, most of the aggregation-promoting mutants did not show major difference…

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Citations

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Metadata

Authors
Mylonas, E., Hascher, A., Bernadó, P., Blackledge, M., Mandelkow, E., & Svergun, D. I.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2008-09-05
Volume
47
Issue
39
Pages
10345-10353
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi800900d
Cited by
218
References
3
Language
en

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