- Abstract:
-
Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. Previously, we discovered that the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers, can be engineered to transition to an ordered and symmetric 48-subunit oligomer by insertion of a peptide from human HspB1 (Hsp27). Here, we uncovered the existence of an array of oligomeric states (30–38 subunits) that can be populated as a consequence ...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 3.3MB)
-
- Publisher copy:
- 10.1016/j.str.2018.05.015
-
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- Funding agency for:
- Chandler, SA
- Funding agency for:
- Benesch, JLP
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 26
- Issue:
- 8
- Pages:
- 1-11
- Publication date:
- 2018-05-18
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- Pubs id:
-
pubs:859120
- URN:
-
uri:b9b9ac13-5fa2-47ca-be46-a364528539b3
- UUID:
-
uuid:b9b9ac13-5fa2-47ca-be46-a364528539b3
- Local pid:
- pubs:859120
- Copyright holder:
- Elsevier ltd.
- Copyright date:
- 2018
- Notes:
- © 2018 Elsevier Ltd. This is the accepted manuscript version of the article. The final version is available online from Elsevier at: https://doi.org/10.1016/j.str.2018.05.015
Journal article
Engineering of a polydisperse small heat-shock protein reveals conserved motifs of oligomer plasticity
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