{"reference": "EMBO J. 2001 Sep 3;20(17):4774-81", "alternative_name": "Cystatin-AS, Stefin-A", "entry": "S-0044", "gene_names": "CSTA, STF1, STFA", "remarks": "Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily", "secondary_structure": "MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF#CCSCCBCCCBSCCHHHHHHHHHHHHHHHHHHTSCCCEEEECCBEEEEEEEEEEEEEEECCTTCCEEEEEEECSTTCGGGCEEEEEECSCCTTSCCSCC&MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF#CCCCCCCCCBTTCHHHHHHHHHHHHHHHHHHCCCCCCCEEEEEEEEEEEEEEEECCEEEESSCCBCCEEEESSTTCSTTEEEEECCCSCCTTSCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "11532941", "ligand_smiles": "", "keyword": "Cystatin A", "peptide_protein_sequence": "chain-ID A: MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF; chain-ID B: MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF", "uniprot_ac": "P01040", "protein_name": "Cystatin-A", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "1N9J", "inchi_key": "", "ec_number": "", "pdb_classification": "HYDROLASE INHIBITOR", "type": "Protein", "author": "Staniforth, R.A., Giannini, S., Higgins, L.D., Conroy, M.J., Hounslow, A.M., Jerala, R., Craven, C.J., Waltho, J.P.", "species": "Homo sapiens", "ligand_id": "", "method": "SOLUTION NMR", "ligand_name": "", "global_stoichiometry": "Homo 2-mer - A2 ", "resolution": "", "ligand_formula": "", "length": "98", "ligstr": "", "description": "Cystatins, an amyloid-forming structural superfamily, form highly stable, domain-swapped dimers at physiological protein concentrations. Destabilization of the folded state shorten the lifetime of the monomeric form. In such circumstances, amyloidogenesis will start from conditions where a domain-swapped dimer is the most prevalent species. Domain swapping occurs by a rearrangement of loop I, generating the new intermonomer interface between strands 2 and 3. Dimerization also occurs when chicken cystatin is in its reduced, molten-globule state, implying that the organization of secondary structure in this state mirrors that in the folded state and that domain swapping is not limited to the folded states of proteins."}