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Structural evaluation of conformational transition state responsible for self-assembly of tau microtubule-binding domain.

Abstract：

:In the brains of Alzheimer's disease patients, the tau protein abnormally aggregates to form an insoluble paired helical filament (PHF). Since the third repeat structure (R3) of the tau microtubule-binding domain plays an essential role in PHF formation and self-aggregates most significantly in an aqueous solution of 20-40% trifluoroethanol (TFE), its possible conformation was estimated from the combination of (i) the TFE-dependent deviations of NH and CalphaH proton chemical shifts from those of the random structure in water and (ii) the TFE-dependent NOE effect connectivity diagrams between the neighboring protons. Consequently, it was indicated that the extended structure of the N-terminal VQIVYK moiety and the alpha-helical-like structure of the LSKVTSKC region provide a structural scaffold for initiating the self-assembled filament formation of the R3 structure. To the best of our knowledge, this is the first study that demonstrated the initial structural moiety and its structural feature necessary for starting the tau PHF formation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Minoura K,Mizushima F,Tokimasa M,Hiraoka S,Tomoo K,Sumida M,Taniguchi T,Ishida T

doi

10.1016/j.bbrc.2004.12.129

subject

Has Abstract

pub_date

2005-02-25 00:00:00

pages

1100-4

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02920-1

journal_volume

327

pub_type

杂志文章

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