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Structure of a strand-swapped dimeric form of CTLA-4Structure of a strand-swapped dimeric form of CTLA-4
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. Domain metastability: a molecular basis for immunoglobulin deposition?,Sonnen AF, Yu C, Evans EJ, Stuart DI, Davis SJ, Gilbert RJ J Mol Biol. 2010 Jun 4;399(2):207-13. Epub 2010 Apr 13. PMID:20394753[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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