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Chaperone-Bound Clients: The Importance of Being Dynamic

Hiller, Sebastian. (2019) Chaperone-Bound Clients: The Importance of Being Dynamic. Trends in Biochemical Sciences, 44 (6). pp. 517-527.

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Abstract

Several recent atomic-resolution studies have resolved how chaperones interact with their client proteins. In some cases, molecular chaperones recognize and bind their clients in conformational ensembles that are locally highly dynamic and interconvert, while in other cases clients bind in unique conformations. The presence of a locally dynamic client ensemble state has important consequences, both for the interpretation of experimental data and for the functionality of chaperones, as local dynamics facilitate rapid client release, folding on and from the chaperone surface, and client recognition without shape complementarity. Facilitated by the local dynamics, at least some chaperones appear to specifically recognize energetically frustrated sites of partially folded client proteins, such that the release of frustration contributes to the interaction affinity.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Elsevier
ISSN:0968-0004
e-ISSN:0167-7640
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:01 Oct 2019 15:28
Deposited On:01 Oct 2019 15:26

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