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Journal article

Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.

Abstract:

The Hsp90 cycle depends on the coordinated activity of a range of cochaperones, including Hop, Hsp70 and peptidyl-prolyl isomerases such as FKBP52. Using mass spectrometry, we investigate the order of addition of these cochaperones and their effects on the stoichiometry and composition of the resulting Hsp90-containing complexes. Our results show that monomeric Hop binds specifically to the Hsp90 dimer whereas FKBP52 binds to both monomeric and dimeric forms of Hsp90. By preforming Hsp90 comp...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.1106261108

Authors


Morgner, N More by this author
Saraiva, MA More by this author
Daturpalli, S More by this author
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
108
Issue:
44
Pages:
17939-17944
Publication date:
2011-11-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:448d1b6d-7284-4e15-a50e-4655c73e2263
Source identifiers:
193137
Local pid:
pubs:193137

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