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Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function.

Abstract:

Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystallin (AAC(59-163)) and human alphaB crystallin (ABC(68-162)), both containing the C-terminal extension that functions in chaperone action and oligomeric assembly. In both structures, the C-terminal extensions swap into neighboring molecules, creatin...

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Publication status:
Published

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Publisher copy:
10.1002/pro.380

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Journal:
Protein science : a publication of the Protein Society More from this journal
Volume:
19
Issue:
5
Pages:
1031-1043
Publication date:
2010-05-01
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
Language:
English
Keywords:
Pubs id:
pubs:59392
UUID:
uuid:b2d1b984-af3b-4607-aaf3-93970bb97222
Local pid:
pubs:59392
Source identifiers:
59392
Deposit date:
2012-12-19

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