4BXL
Structure of alpha-synuclein in complex with an engineered binding protein
Summary for 4BXL
| Entry DOI | 10.2210/pdb4bxl/pdb |
| Descriptor | AS69, ALPHA SYNUCLEIN (2 entities in total) |
| Functional Keywords | fibril, amyloid, parkinson's disease, protein aggregation, protein engineering, protein misfolding, scaffold proteins |
| Biological source | SYNTHETIC CONSTRUCT More |
| Cellular location | Cytoplasm: P37840 |
| Total number of polymer chains | 3 |
| Total formula weight | 12380.70 |
| Authors | Mirecka, E.A.,Shaykhalishahi, H.,Lecher, J.,Stoldt, M.,Hoyer, W. (deposition date: 2013-07-12, release date: 2014-05-21, Last modification date: 2024-10-09) |
| Primary citation | Mirecka, E.A.,Shaykhalishahi, H.,Gauhar, A.,Akgul, S.,Lecher, J.,Willbold, D.,Stoldt, M.,Hoyer, W. Sequestration of a Beta-Hairpin for Control of Alpha-Synuclein Aggregation. Angew.Chem.Int.Ed.Engl., 53:4227-, 2014 Cited by PubMed Abstract: The misfolding and aggregation of the protein α-synuclein (α-syn), which results in the formation of amyloid fibrils, is involved in the pathogenesis of Parkinson's disease and other synucleinopathies. The emergence of amyloid toxicity is associated with the formation of partially folded aggregation intermediates. Here, we engineered a class of binding proteins termed β-wrapins (β-wrap proteins) with affinity for α-synuclein (α-syn). The NMR structure of an α-syn:β-wrapin complex reveals a β-hairpin of α-syn comprising the sequence region α-syn(37-54). The β-wrapin inhibits α-syn aggregation and toxicity at substoichiometric concentrations, demonstrating that it interferes with the nucleation of aggregation. PubMed: 24623599DOI: 10.1002/ANIE.201309001 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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