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Chaperone-client complexes: A dynamic liaison.

Review article
Authors Sebastian Hiller
Björn Marcus Burmann
Published in Journal of magnetic resonance (San Diego, Calif. : 1997)
Volume 289
Pages 142-155
ISSN 1096-0856
Publication year 2018
Published at Department of Chemistry and Molecular Biology
Pages 142-155
Language en
Links dx.doi.org/10.1016/j.jmr.2017.12.00...
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Structural Biology

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.

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