{"resolution": "1.45", "ligand_mw": "", "secondary_structure": "GNLVS#CCCCC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P13727", "remarks": "Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)", "description": "Following eosinophil activation, MBP-1 toxicity is triggered by granule acidification, followed by extracellular aggregation, which mediates the damage to pathogens and host cells. Larger non-toxic amyloid plaques are also present in tissues of eosinophilic patients in a feedback mechanism that likely limits tissue damage under pathological conditions of MBP-1 oversecretion. Our results suggest that MBP-1 aggregation is important for innate immunity and immunopathology mediated by eosinophils and clarify how its polymorphic self-association pathways regulate toxicity intra- and extracellularly. ", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "Bone marrow proteoglycan", "ligstr": "", "pmid": "25728769", "mutation_s_field": "No", "author": "Soragni, A., Yousefi, S., Stoeckle, C., Soriaga, A.B., Sawaya, M.R., Kozlowski, E., Schmid, I., Radonjic-Hoesli, S., Boutet, S., Williams, G.J., Messerschmidt, M., Seibert, M.M., Cascio, D., Zatsepin, N.A., Burghammer, M., Riekel, C., Colletier, J.P., Rie", "pdb_id": "4QXX", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.192", "protein_name": "Bone marrow proteoglycan", "gene_names": "", "global_stoichiometry": "Homo 6-mer - A6 ", "alternative_name": "", "peptide_protein_sequence": "chain-ID Z: GNLVS", "pdb_classification": "PROTEIN FIBRIL", "reference": "Mol Cell. 2015 Mar 19;57(6):1011-1021.", "length": "5", "entry": "S-0374"}