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J Mol Biol. 2010 Jun 4;399(2):207-13. doi: 10.1016/j.jmb.2010.04.011. Epub 2010 Apr 13.

Domain metastability: a molecular basis for immunoglobulin deposition?

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1
Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. andreas@strubi.ox.ac.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.

PMID:
20394753
PMCID:
PMC2954335
DOI:
10.1016/j.jmb.2010.04.011
[Indexed for MEDLINE]
Free PMC Article
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