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 PubMed
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.
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
- ↑ Sonnen AF, Yu C, Evans EJ, Stuart DI, Davis SJ, Gilbert RJ. Domain metastability: a molecular basis for immunoglobulin deposition? J Mol Biol. 2010 Jun 4;399(2):207-13. Epub 2010 Apr 13. PMID:20394753 doi:10.1016/j.jmb.2010.04.011
