Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones

He, Lichun and Hiller, Sebastian. (2019) Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones. Chembiochem : a European journal of chemical biology, 20 (22). pp. 2803-2806.

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Molecular chaperones are crucial for cellular life to ensure that all proteins obtain their right fold and functionality. Many chaperones promiscuously bind a wide spectrum of client proteins, ranging from nascent to quasi-native and native proteins. Several recent studies have investigated, at atomic resolution, how chaperones interact with native proteins. Native proteins feature a wide variety of structural conformations, and therefore, a given chaperone cannot accomplish full surface complementarity to all of its client proteins. This limitation is circumvented by the recognition of frustrated regions on the client protein surface by the chaperone. In this interaction mode, the chaperone forms a multitude of transient local interactions with some segments of the client, whereas other parts are transiently not in favorable interactions. A permanent rearrangement of the client conformation on the chaperone occurs. Reconfiguration on the chaperone surface also gives the client a chance to fold into its correct, minimally frustrated conformation.
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
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:10 Feb 2020 16:36
Deposited On:10 Feb 2020 16:36

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