|2x44, resolution 2.60Å ()|
|Related:||1ah1, 1h6e, 1i8l, 1i85|
STRUCTURE OF A STRAND-SWAPPED DIMERIC FORM OF CTLA-4
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.