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We 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.

Original publication

DOI

10.1016/j.jmb.2010.04.011

Type

Journal article

Journal

J Mol Biol

Publication Date

04/06/2010

Volume

399

Pages

207 - 213

Keywords

Amyloid, Antigens, CD, CTLA-4 Antigen, Crystallography, X-Ray, Dimerization, Humans, Immunoglobulin Light Chains, Macromolecular Substances, Microscopy, Electron, Models, Molecular, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary