{"reference": "Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):16938-43.", "alternative_name": "", "entry": "S-0181", "gene_names": "", "remarks": "Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1", "secondary_structure": "MVGGVVIA#CEEEEEEC&MVGGVVIA#CEEEEEEC&MVGGVVIA#CEEEEEEC&MVGGVVIA#CEEEEEEC&MVGGVVIA#CBCCEEEC&MVGGVVIA#CBCCEEEC&MVGGVVIA#CBCCEEEC&MVGGVVIA#CBCCEEEC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "21949245", "ligand_smiles": "", "keyword": "AMYLOID BETA A4 PROTEIN", "peptide_protein_sequence": "chain-ID A: MVGGVVIA; chain-ID B: MVGGVVIA; chain-ID C: MVGGVVIA; chain-ID D: MVGGVVIA; chain-ID E: MVGGVVIA; chain-ID F: MVGGVVIA; chain-ID G: MVGGVVIA; chain-ID H: MVGGVVIA", "uniprot_ac": "P05067", "protein_name": "Amyloid-beta A4 protein", "r_value_free": "0.231", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "2Y3K", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Colletier, J., Laganowsky, A., Landau, M., Zhao, M., Soriaga, A.B., Goldschmidt, L., Flot, D., Cascio, D., Sawaya, M.R., Eisenberg, D.", "species": "Homo sapiens", "ligand_id": "", "method": "X-RAY DIFFRACTION", "ligand_name": "", "global_stoichiometry": "Homo 2-mer - A2", "resolution": "1.9", "ligand_formula": "", "length": "8", "ligstr": "", "description": "ABeta molecules form Beta-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of ABeta has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. They determined eight new microcrystal structures of fiber-forming segments of ABeta. These structures, all of short, self-complementing pairs of Beta-sheets termed steric zippers, reveal a variety of modes of self-association of ABeta. "}