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Domain metastability: a molecular basis for immunoglobulin deposition?

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.
Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2010.04.011

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
Weatherall Insti. of Molecular Medicine
Role:
Author
Journal:
Journal of molecular biology More from this journal
Volume:
399
Issue:
2
Pages:
207-213
Publication date:
2010-06-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:53307
UUID:
uuid:2230d18f-f86b-4854-9c8d-6e2e2d779808
Local pid:
pubs:53307
Source identifiers:
53307
Deposit date:
2012-12-19

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