{"reference": "Nat Chem. 2018 Feb;10(2):170-176.", "alternative_name": "", "entry": "S-0470", "gene_names": "", "remarks": "KVQIINKKLD, Structure of the amyloid spine from microtubule associated protein tau Repeat 2", "secondary_structure": "KVQIINKKLD#CCCCCCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "29359764", "ligand_smiles": "", "keyword": "Microtubule-associated protein tau", "peptide_protein_sequence": "chain-ID A: KVQIINKKLD", "uniprot_ac": "P10636", "protein_name": "Microtubule-associated protein tau", "r_value_free": "0.213", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "5V5B", "inchi_key": "", "ec_number": "", "pdb_classification": "STRUCTURAL PROTEIN", "type": "Fibril", "author": "Seidler, P.M., Boyer, D.R., Rodriguez, J.A., Sawaya, M.R., Cascio, D., Murray, K., Gonen, T., Eisenberg, D.S.", "species": "Homo sapiens", "ligand_id": "", "method": "ELECTRON CRYSTALLOGRAPHY", "ligand_name": "", "global_stoichiometry": "Homo 18-mer - A18", "resolution": "1.5", "ligand_formula": "", "length": "10", "ligstr": "", "description": "They show that the VQIINK segment is the more powerful driver of tau aggregation. Two structures of this segment determined by the cryo-electron microscopy method explain its dominant influence on tau aggregation. Of practical significance, the structures lead to the design of inhibitors that not only inhibit tau aggregation but also inhibit the ability of exogenous full-length tau fibrils to seed intracellular tau in HEK293 biosensor cells into amyloid."}