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Domain Metastability: A Molecular Basis for Immunoglobulin Deposition? |
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| Authors: | Andreas F-P Sonnen Chao Yu David I Stuart Robert JC Gilbert |
| Institution: | 1 Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK 2 Nuffield Department of Clinical Medicine and MRC Human Immunology Unit, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK |
| Abstract: | 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. |
| Keywords: | IgSF Ig superfamily TFE 2 2 2-trifluoroethanol PBS phosphate-buffered saline |
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