5LFY
Zinc bound dimer of the fragment of human amyloid-beta peptide with Alzheimer's disease pathogenic Taiwanese mutation D7H
Summary for 5LFY
| Entry DOI | 10.2210/pdb5lfy/pdb |
| NMR Information | BMRB: 34019 |
| Descriptor | Amyloid beta A4 protein, ZINC ION (2 entities in total) |
| Functional Keywords | alzheimer's disease, amyloid-beta peptide, zinc complex, zinc-bound dimer, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 2569.35 |
| Authors | Polshakov, V.I.,Mantsyzov, A.B.,Kozin, S.A. (deposition date: 2016-07-05, release date: 2017-08-23, Last modification date: 2024-11-13) |
| Primary citation | Polshakov, V.I.,Mantsyzov, A.B.,Kozin, S.A.,Adzhubei, A.A.,Zhokhov, S.S.,van Beek, W.,Kulikova, A.A.,Indeykina, M.I.,Mitkevich, V.A.,Makarov, A.A. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-beta Fragment with Taiwanese Mutation D7H. Angew. Chem. Int. Ed. Engl., 56:11734-11739, 2017 Cited by PubMed Abstract: Zinc-induced oligomerization of amyloid-β peptide (Aβ) produces potentially pathogenic agents of Alzheimer's disease. Mutations and modifications in the metal binding domain 1-16 of Aβ peptide crucially affect its zinc-induced oligomerization by changing intermolecular zinc mediated interface. The 3D structure of this interface appearing in a range of Aβ species is a prospective drug target for disease modifying therapy. Using NMR spectroscopy, EXAFS spectroscopy, mass spectrometry, and isothermal titration calorimetry the interaction of zinc ions with Aβ fragments 1-7 and 1-10 carrying familial Taiwanese mutation D7H was studied. Zinc ions induce formation of a stable homodimer formed by the two peptide chains fastened by two zinc ions and stacking interactions of imidazole rings. A binuclear zinc interaction fold in the dimer structure was discovered. It can be used for designing zinc-regulated proteins and zinc-mediated self-assembling peptides. PubMed: 28570778DOI: 10.1002/anie.201704615 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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