PDBsum entry 2mz7

Protein binding

PDB id: 2mz7

Contents

Protein chain

46 a.a.

PDB id:

2mz7

Name:

Protein binding

Title:

Structure of tau(267-312) bound to microtubules

Structure:

Microtubule-associated protein tau. Chain: a. Fragment: unp residues 584-629. Synonym: neurofibrillary tangle protein, paired helical filament-tau, phf-tau. Engineered: yes

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

20 models

Authors:

H.Kadavath,M.Jaremko,L.Jaremko,M.Zweckstetter

Key ref:

H.Kadavath et al. (2015). Folding of the Tau Protein on Microtubules. Angew Chem Int Ed Engl, 54, 10347-10351. PubMed id: 26094605 DOI: 10.1002/anie.201501714

Date:

06-Feb-15 Release date: 08-Jul-15

Protein chain

P10636  (TAU_HUMAN) -  Microtubule-associated protein tau from Homo sapiens

Seq: 758 a.a.

Struc: 46 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/anie.201501714

Angew Chem Int Ed Engl 54:10347-10351 (2015)

PubMed id: 26094605

Folding of the Tau Protein on Microtubules.

H.Kadavath, M.Jaremko, �.�.Jaremko, J.Biernat, E.Mandelkow, M.Zweckstetter.

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.