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L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers.

Abstract:

Transthyretin is a tetrameric protein associated with the commonest form of systemic amyloid disease. Using isotopically labeled proteins and mass spectrometry, we compared subunit exchange in wild-type transthyretin with that of the variant associated with the most aggressive form of the disease, L55P. Wild-type subunit exchange occurs via both monomers and dimers, whereas exchange via dimers is the dominant mechanism for the L55P variant. Because patients with the L55P mutation are heterozy...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m508753200

Authors


Keetch, CA More by this author
Bromley, EH More by this author
McCammon, MG More by this author
Christodoulou, J More by this author
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Journal:
The Journal of biological chemistry
Volume:
280
Issue:
50
Pages:
41667-41674
Publication date:
2005-12-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:65a2b761-73e8-4d6a-8005-007d335cf580
Source identifiers:
59278
Local pid:
pubs:59278

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