 |
PDBsum entry 2mz7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
2mz7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Folding of the tau protein on microtubules.
|
|
|
Authors
|
|
H.Kadavath,
M.Jaremko,
..Jaremko,
J.Biernat,
E.Mandelkow,
M.Zweckstetter.
|
|
|
Ref.
|
|
Angew Chem Int Ed Engl, 2015,
54,
10347-10351.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Microtubules are regulated by microtubule-associated proteins. However, little
is known about the structure of microtubule-associated proteins in complex with
microtubules. Herein we show that the microtubule-associated protein Tau, which
is intrinsically disordered in solution, locally folds into a stable structure
upon binding to microtubules. While Tau is highly flexible in solution and
adopts a β-sheet structure in amyloid fibrils, in complex with microtubules the
conserved hexapeptides at the beginning of the Tau repeats two and three convert
into a hairpin conformation. Thus, binding to microtubules stabilizes a unique
conformation in Tau.
|
|
|
|
|
|
|
