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Chaperone-client complexes: A dynamic liaison

Hiller, Sebastian and Burmann, Björn M.. (2018) Chaperone-client complexes: A dynamic liaison. Journal of Magnetic Resonance, 289. pp. 142-155.

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Official URL: http://edoc.unibas.ch/57631/

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Abstract

Living cells contain molecular chaperones that are organized in intricate networks to surveil protein homeostasis by avoiding polypeptide misfolding, aggregation, and the generation of toxic species. In addition, cellular chaperones also fulfill a multitude of alternative functionalities: transport of clients towards a target location, help them fold, unfold misfolded species, resolve aggregates, or deliver clients towards proteolysis machineries. Until recently, the only available source of atomic resolution information for virtually all chaperones were crystal structures of their client-free, apo-forms. These structures were unable to explain details of the functional mechanisms underlying chaperone-client interactions. The difficulties to crystallize chaperones in complexes with clients arise from their highly dynamic nature, making solution NMR spectroscopy the method of choice for their study. With the advent of advanced solution NMR techniques, in the past few years a substantial number of structural and functional studies on chaperone-client complexes have been resolved, allowing unique insight into the chaperone -client interaction. This review summarizes the recent insights provided by advanced high resolution NMR-spectroscopy to understand chaperone-client interaction mechanisms at the atomic scale.
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:1090-7807
e-ISSN:1096-0856
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:15 May 2018 15:56
Deposited On:15 May 2018 15:56

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