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Domain metastability: a molecular basis for immunoglobulin deposition?Sonnen AF; Yu C; Evans EJ; Stuart DI; Davis SJ; Gilbert RJJ Mol Biol 2010[Jun]; 399 (2): 207-13We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits.|Amyloid/chemistry/metabolism[MESH]|Antigens, CD/*chemistry/metabolism[MESH]|CTLA-4 Antigen[MESH]|Crystallography, X-Ray[MESH]|Dimerization[MESH]|Humans[MESH]|Immunoglobulin Light Chains/*chemistry/metabolism[MESH]|Macromolecular Substances/chemistry[MESH]|Microscopy, Electron[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Protein Structure, Quaternary[MESH]|Protein Structure, Tertiary[MESH] |
