2MZ7
Structure of Tau(267-312) bound to Microtubules
Summary for 2MZ7
| Entry DOI | 10.2210/pdb2mz7/pdb |
| Related | 2MNK 2MNL 2MNM 2MNN 2MNO 2MNP |
| NMR Information | BMRB: 25475 |
| Descriptor | Microtubule-associated protein tau (1 entity in total) |
| Functional Keywords | tau, microtubule, dynamics, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytosol : P10636 |
| Total number of polymer chains | 1 |
| Total formula weight | 4892.68 |
| Authors | Kadavath, H.,Jaremko, M.,Jaremko, L.,Zweckstetter, M. (deposition date: 2015-02-06, release date: 2015-07-08, Last modification date: 2024-05-15) |
| Primary citation | Kadavath, H.,Jaremko, M.,Jaremko, M.,Biernat, J.,Mandelkow, E.,Zweckstetter, M. Folding of the Tau Protein on Microtubules. Angew.Chem.Int.Ed.Engl., 54:10347-10351, 2015 Cited by PubMed 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. PubMed: 26094605DOI: 10.1002/anie.201501714 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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