{"reference": "Nat Struct Mol Biol. 2018 Jun;25(6):463-471.", "alternative_name": "", "entry": "S-0491", "gene_names": "", "remarks": "Crystal structure of the segment, GNNQGSN, from the low complexity domain of TDP-43, residues 300-306", "secondary_structure": "GNNQGSN#CCCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "29786080", "ligand_smiles": "", "keyword": "TAR DNA-binding protein 43", "peptide_protein_sequence": "chain-ID A: GNNQGSN", "uniprot_ac": "Q13148", "protein_name": "TAR DNA-binding protein 43", "r_value_free": "0.195", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "5WKD", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Guenther, E.L., Cao, Q., Trinh, H., Lu, J., Sawaya, M.R., Cascio, D., Boyer, D.R., Rodriguez, J.A., Hughes, M.P., Eisenberg, D.S.", "species": "Homo sapiens", "ligand_id": "", "method": "X-RAY DIFFRACTION", "ligand_name": "", "global_stoichiometry": "Homo 10-mer - A10", "resolution": "1.8", "ligand_formula": "", "length": "7", "ligstr": "", "description": "To uncover the structural origins of two modes of Beta-sheet-rich aggregation (reversible stress granules and irreversible pathogenic amyloid), they have determined ten structures of segments of the LCD of human TDP-43. Six of these segments form steric zippers characteristic of the spines of pathogenic amyloid fibrils; four others form LARKS, the labile amyloid-like interactions characteristic of protein hydrogels and proteins found in membraneless organelles, including stress granules. Segments 300GNNQGSN306, 328AALQSS333 and 370GNNSYS375 all form Class 1 steric zippers in which the Beta-sheets are mated face-to-face with the same edges of the sheet oriented up the fibril."}