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Engineering of a polydisperse small heat-shock protein reveals conserved motifs of oligomer plasticity

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 ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1016/j.str.2018.05.015

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chemistry
Role:
Author
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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

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