{"reference": "Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18119-24. Epub  2006 Nov 15", "alternative_name": "", "entry": "S-0095", "gene_names": "B2M, CDABP0092, HDCMA22P", "remarks": "3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR", "secondary_structure": "SNFLNCYVSGFHPSDIEVDLLK#CCEEEEEESCCCSSEEEEEECC&SNFLNCYVSGFHPSDIEVDLLK#CCEEEEEECCCSSCEEEEEECC&SNFLNCYVSGFHPSDIEVDLLK#CCEEEEEESCCSSCEEEEEECC&SNFLNCYVSGFHPSDIEVDLLK#CCEEEEEECCCCSSEEEEEETC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "17108084", "ligand_smiles": "", "keyword": "Beta-2-microglobulin", "peptide_protein_sequence": "chain-ID A: SNFLNCYVSGFHPSDIEVDLLK; chain-ID B: SNFLNCYVSGFHPSDIEVDLLK; chain-ID C: SNFLNCYVSGFHPSDIEVDLLK; chain-ID D: SNFLNCYVSGFHPSDIEVDLLK", "uniprot_ac": "P61769", "protein_name": "Beta-2-microglobulin", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "2E8D", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Iwata, K., Fujiwara, T., Matsuki, Y., Akutsu, H., Takahashi, S., Naiki, H., Goto, Y.", "species": "Homo sapiens", "ligand_id": "", "method": "SOLID-STATE NMR", "ligand_name": "", "global_stoichiometry": "Homo 4-mer - A4 ", "resolution": "", "ligand_formula": "", "length": "22", "ligstr": "", "description": "solid-state NMR, x-ray fiber diffraction, and atomic force microscopy were combined to reveal the 3D structure of amyloid protofilament-like fibrils formed by a 22-residue K3 peptide (Ser(20)-Lys(41)) of Beta(2)-microglobulin, a protein responsible for dialysis-related amyloidosis. The conformation of K3 fibrils was found to be a Beta-strand-loop-Beta-strand with each K3 molecule stacked in a parallel and staggered manner. It is suggested that the fibrillar conformation is stabilized by intermolecular interactions, rather than by intramolecular hydrophobic packing as seen in globular proteins."}